Complement-associated protein SP-40,40
Complement cytolysis inhibitor
CLI
NA1/NA2
Apolipoprotein J
Apo-J
Testosterone-repressed prostate message 2
TRPM-2
Ku70-binding protein 1
Aging-associated gene 4 protein

Contains

Clusterin beta chain
     (ApoJalpha)
     (Complement cytolysis inhibitor a chain)
Clusterin alpha chain
     (ApoJbeta)
     (Complement cytolysis inhibitor b chain)

Gene name

	Name:	CLU
	Synonyms:	APOJ, CLI, KUB1
	ORFNames:	AAG4

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Liver; PubMed=2721499 [NCBI, ExPASy, EBI, Israel, Japan] Kirszbaum L., Sharpe J.A., Murphy B., D'Apice J.F.A., Classon B., Hudson P., Walker I.D.; "Molecular cloning and characterization of the novel, human complement-associated protein, SP-40,40: a link between the complement and reproductive systems."; EMBO J. 8:711-718(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1021/bi00474a025; PubMed=1974459 [NCBI, ExPASy, EBI, Israel, Japan] de Silva H.V., Harmony J.A.K., Stuart W.D., Gil C.M., Robbins J.; "Apolipoprotein J: structure and tissue distribution."; Biochemistry 29:5380-5389(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. DOI=10.1111/j.1432-1033.1994.tb18807.x; PubMed=8181474 [NCBI, ExPASy, EBI, Israel, Japan] Wong P., Taillefer D., Lakins J., Pineault J., Chader G., Tenniswood M.; "Molecular characterization of human TRPM-2/clusterin, a gene associated with sperm maturation, apoptosis and neurodegeneration."; Eur. J. Biochem. 221:917-925(1994).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Kim J.W.; "Identification of human aging-associated gene."; Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Small intestine; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-317; ASN-328 AND LEU-396. NIEHS SNPs program; Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature04406; PubMed=16421571 [NCBI, ExPASy, EBI, Israel, Japan] Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.; "DNA sequence and analysis of human chromosome 8."; Nature 439:331-335(2006).
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[10]	NUCLEOTIDE SEQUENCE [MRNA] OF 2-449. DOI=10.1073/pnas.86.18.7123; PubMed=2780565 [NCBI, ExPASy, EBI, Israel, Japan] Jenne D.E., Tschopp J.; "Molecular structure and functional characterization of a human complement cytolysis inhibitor found in blood and seminal plasma: identity to sulfated glycoprotein 2, a constituent of rat testis fluid."; Proc. Natl. Acad. Sci. U.S.A. 86:7123-7127(1989).
[11]	PROTEIN SEQUENCE OF 23-33; 229-242; 303-317 AND 397-403. PubMed=1903064 [NCBI, ExPASy, EBI, Israel, Japan] James R.W., Hochstrasser A.-C., Borghini I., Martin B.M., Pometta D., Hochstrasser D.F.; "Characterization of a human high density lipoprotein-associated protein, NA1/NA2. Identity with SP-40,40, an inhibitor of complement-mediated cytolysis."; Arterioscler. Thromb. 11:645-652(1991).
[12]	PROTEIN SEQUENCE OF 23-52 AND 228-257. PubMed=2387851 [NCBI, ExPASy, EBI, Israel, Japan] de Silva H., Stuart W.D., Park Y.B., Mao S.J.T., Gil C.M., Wetterau J.R., Busch S.J., Harmony J.A.K.; "Purification and characterization of apolipoprotein J."; J. Biol. Chem. 265:14292-14297(1990).
[13]	PROTEIN SEQUENCE OF 23-41 AND 228-246. PubMed=8328966 [NCBI, ExPASy, EBI, Israel, Japan] Ghiso J., Matsubara E., Koudinov A., Choi-Miura N.-H., Tomita M., Wisniewski T., Frangione B.; "The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex."; Biochem. J. 293:27-30(1993).
[14]	PROTEIN SEQUENCE OF 23-37 AND 228-242. DOI=10.1016/0161-5890(89)90139-9; PubMed=2601725 [NCBI, ExPASy, EBI, Israel, Japan] Choi N.H., Mazda T., Tomita M.; "A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytes."; Mol. Immunol. 26:835-840(1989).
[15]	PROTEIN SEQUENCE OF 23-33 AND 228-240. PubMed=3154963 [NCBI, ExPASy, EBI, Israel, Japan] Hochstrasser A.-C., James R.W., Martin B.M., Harrington M., Hochstrasser D.F., Pometta D., Merril C.R.; "HDL particle associated proteins in plasma and cerebrospinal fluid: identification and partial sequencing."; Appl. Theor. Electrophor. 1:73-76(1988).
[16]	NUCLEOTIDE SEQUENCE [MRNA] OF 61-449. TISSUE=Astrocytoma; DOI=10.1073/pnas.88.19.8577; PubMed=1924317 [NCBI, ExPASy, EBI, Israel, Japan] Danik M., Chabot J.G., Mercier C., Benabid A.L., Chauvin C., Quirion R., Suh M.; "Human gliomas and epileptic foci express high levels of a mRNA related to rat testicular sulfated glycoprotein 2, a purported marker of cell death."; Proc. Natl. Acad. Sci. U.S.A. 88:8577-8581(1991).
[17]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-449. TISSUE=Fetal liver; Glew M.D., Kirszbaum L., Bozas S.E., Walker I.D.; Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[18]	PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374. DOI=10.1016/0014-5793(92)80330-J; PubMed=1551440 [NCBI, ExPASy, EBI, Israel, Japan] Kirszbaum L., Bozas S.E., Walker I.D.; "SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges."; FEBS Lett. 297:70-76(1992).
[19]	INTERACTION WITH APOA1. DOI=10.1016/0005-2760(91)90167-G; PubMed=1742316 [NCBI, ExPASy, EBI, Israel, Japan] Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J., Murphy B., Walker I.D.; "The apolipoprotein A-I binding protein of placenta and the SP-40,40 protein of human blood are different proteins which both bind to apolipoprotein A-I."; Biochim. Biophys. Acta 1086:255-260(1991).
[20]	DISULFIDE BONDS. PubMed=1491011 [NCBI, ExPASy, EBI, Israel, Japan] Choi-Miura N.H., Takahashi Y., Nakano Y., Tobe T., Tomita M.; "Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J)."; J. Biochem. 112:557-561(1992).
[21]	INTERACTION WITH PON1. DOI=10.1021/bi00169a026; PubMed=8292612 [NCBI, ExPASy, EBI, Israel, Japan] Kelso G.J., Stuart W.D., Richter R.J., Furlong C.E., Jordan-Starck T.C., Harmony J.A.K.; "Apolipoprotein J is associated with paraoxonase in human plasma."; Biochemistry 33:832-839(1994).
[22]	GLYCOSYLATION AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374. PubMed=9336835 [NCBI, ExPASy, EBI, Israel, Japan] Kapron J.T., Hilliard G.M., Lakins J.N., Tenniswood M.P., West K.A., Carr S.A., Crabb J.W.; "Identification and characterization of glycosylation sites in human serum clusterin."; Protein Sci. 6:2120-2133(1997).
[23]	GLYCOSYLATION AT ASN-354. DOI=10.1038/nbt827; PubMed=12754519 [NCBI, ExPASy, EBI, Israel, Japan] Zhang H., Li X.-J., Martin D.B., Aebersold R.; "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."; Nat. Biotechnol. 21:660-666(2003).
[24]	INTERACTION WITH CLUAP1. DOI=10.1038/sj.onc.1208100; PubMed=15480429 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi M., Lin Y.-M., Nakamura Y., Furukawa Y.; "Isolation and characterization of a novel gene CLUAP1 whose expression is frequently upregulated in colon cancer."; Oncogene 23:9289-9294(2004).
[25]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-354 AND ASN-374, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan] Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."; Proteomics 4:454-465(2004).
[26]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145; ASN-291; ASN-354 AND ASN-374, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[27]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, AND MASS SPECTROMETRY. TISSUE=Saliva; DOI=10.1021/pr050492k; PubMed=16740002 [NCBI, ExPASy, EBI, Israel, Japan] Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.; "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."; J. Proteome Res. 5:1493-1503(2006).
[28]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-374, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan] Lewandrowski U., Moebius J., Walter U., Sickmann A.; "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."; Mol. Cell. Proteomics 5:226-233(2006).
[29]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-291; ASN-317 AND ASN-374, AND MASS SPECTROMETRY. TISSUE=Milk; DOI=10.1002/pmic.200701057; PubMed=18780401 [NCBI, ExPASy, EBI, Israel, Japan] Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."; Proteomics 8:3833-3847(2008).
[30]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-103; ASN-145; ASN-354 AND ASN-374, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).

Comments

FUNCTION: Not yet clear. It is known to be expressed in a variety of tissues and it seems to be able to bind to cells, membranes and hydrophobic proteins. It has been associated with programmed cell death (apoptosis).
SUBUNIT: Antiparallel disulfide-linked heterodimer. Interacts with APOA1, CLUAP1 AND PON1.
INTERACTION:
Q9NRI5:DISC1; NbExp=2; IntAct=EBI-1104674, EBI-529989;
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the clusterin family.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/clu/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X14723; CAA32847.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02908; AAA51765.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63379; AAB06507.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63376; AAB06507.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63377; AAB06507.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63378; AAB06507.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M64722; AAB06508.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY513288; AAT08041.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK313870; BAG36598.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX648414; CAI45990.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY341244; AAP88927.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BC010514; AAH10514.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019588; AAH19588.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M25915; AAA35692.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M74816; AAA60321.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00974; AAA60567.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00291262; -.

PIR

S43646; A41386.

RefSeq

NP_001822.2; -.
NP_976084.1; -.

UniGene

Hs.436657

3D structure databases

ModBase

P10909.

Protein-protein interaction databases

IntAct

P10909; 6.

Enzyme and pathway databases

Reactome

REACT_604; Hemostasis.

2D gel databases

P10909; -.

P10909; -.

P10909; -.

P10909; -.

IPI00291262; -.

Organism-specific databases

GC08M027510; -.

HIX0007408; -.

HGNC:2095; CLU.

CLU.

CAB000476; -.
CAB016253; -.
HPA000572; -.

MIM

185430; gene. [NCBI / EBI]

PharmGKB

PA26620; -.

Gene expression databases

P10909; -.

P10909; -.

HS_CLU; -.

ENSG00000120885; Homo sapiens.

Ontologies

GO:0034366;	Cellular component: spherical high-density lipoprotein particle (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006958;	Biological process: complement activation, classical pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0045087;	Biological process: innate immune response (inferred from electronic annotation from UniProtKB-KW).
GO:0006629;	Biological process: lipid metabolic process (non-traceable author statement from ProtInc).
GO:0043691;	Biological process: reverse cholesterol transport (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR016016; Clusterin.
IPR000753; Clusterin-like.
IPR016015; Clusterin_C.
IPR016014; Clusterin_N.
Graphical view of domain structure.

PANTHER

PTHR10970:SF1; Clusterin; 1.

Pfam

PF01093; Clusterin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002368; Clusterin; 1.

SMART

SM00035; CLa; 1.
SM00030; CLb; 1.
SMART graphical view of domain structure.

PROSITE

PS00492; CLUSTERIN_1; 1.
PS00493; CLUSTERIN_2; 1.

Proteomic databases

PRIDE

P10909; -.

Genome annotation databases

Ensembl

ENSG00000120885; Homo sapiens. [Contig view]

GeneID

1191; -.

KEGG

hsa:1191; -.

Phylogenomic databases

HOGENOM

P10909; -.

HOVERGEN

P10909; -.

Other

4922; -.

P10909; -.

CLU; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Apoptosis; Complement pathway; Direct protein sequencing; Disulfide bond; Glycoprotein; Immune response; Innate immunity; Polymorphism; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`
`CHAIN`	`23 449`	`427`	`Clusterin.`	`PRO_0000005529`
`CHAIN`	`23 227`	`205`	`Clusterin beta chain.`	`PRO_0000005530`
`CHAIN`	`228 449`	`222`	`Clusterin alpha chain.`	`PRO_0000005531`
`CARBOHYD`	`86 86`		`N-linked (GlcNAc...).`
`CARBOHYD`	`103 103`		`N-linked (GlcNAc...).`
`CARBOHYD`	`145 145`		`N-linked (GlcNAc...).`
`CARBOHYD`	`291 291`		`N-linked (GlcNAc...).`
`CARBOHYD`	`317 317`		`N-linked (GlcNAc...).`
`CARBOHYD`	`354 354`		`N-linked (GlcNAc...).`
`CARBOHYD`	`374 374`		`N-linked (GlcNAc...).`
`DISULFID`	`102 313`		`Interchain (between beta and alpha chains).`
`DISULFID`	`113 305`		`Interchain (between beta and alpha chains).`
`DISULFID`	`116 302`		`Interchain (between beta and alpha chains).`
`DISULFID`	`121 295`		`Interchain (between beta and alpha chains).`
`DISULFID`	`129 285`		`Interchain (between beta and alpha chains).`
`VARIANT`	`317 317`	`1`	`N -> H (in dbSNP:rs9331936 [NCBI]).`	`VAR_019366`
`VARIANT`	`328 328`	`1`	`D -> N (in dbSNP:rs9331938 [NCBI]).`	`VAR_019367`
`VARIANT`	`396 396`	`1`	`S -> L (in dbSNP:rs13494 [NCBI]).`	`VAR_019368`
`CONFLICT`	`28 28`		`D -> S (in Ref. 11; AA sequence and 15; AA sequence).`
`CONFLICT`	`47 47`		`Q -> H (in Ref. 12; AA sequence).`
`CONFLICT`	`52 52`		`G -> Q (in Ref. 12; AA sequence).`
`CONFLICT`	`172 172`		`M -> V (in Ref. 9; CAI45990).`
`CONFLICT`	`224 224`		`R -> L (in Ref. 5; BAG36598).`
`CONFLICT`	`305 305`		`C -> M (in Ref. 11; AA sequence).`
`CONFLICT`	`388 388`		`T -> M (in Ref. 9; CAI45990).`
`CONFLICT`	`411 411`		`D -> G (in Ref. 5; BAG36598).`

Sequence information

Length: 449 AA [This is the length of the unprocessed precursor]

Molecular weight: 52495 Da [This is the MW of the unprocessed precursor]

CRC64: 9583DE4CCECC169F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMKTLLLFVG LLLTWESGQV LGDQTVSDNE LQEMSNQGSK YVNKEIQNAV NGVKQIKTLI 

        70         80         90        100        110        120 
EKTNEERKTL LSNLEEAKKK KEDALNETRE SETKLKELPG VCNETMMALW EECKPCLKQT 

       130        140        150        160        170        180 
CMKFYARVCR SGSGLVGRQL EEFLNQSSPF YFWMNGDRID SLLENDRQQT HMLDVMQDHF 

       190        200        210        220        230        240 
SRASSIIDEL FQDRFFTREP QDTYHYLPFS LPHRRPHFFF PKSRIVRSLM PFSPYEPLNF 

       250        260        270        280        290        300 
HAMFQPFLEM IHEAQQAMDI HFHSPAFQHP PTEFIREGDD DRTVCREIRH NSTGCLRMKD 

       310        320        330        340        350        360 
QCDKCREILS VDCSTNNPSQ AKLRRELDES LQVAERLTRK YNELLKSYQW KMLNTSSLLE 

       370        380        390        400        410        420 
QLNEQFNWVS RLANLTQGED QYYLRVTTVA SHTSDSDVPS GVTEVVVKLF DSDPITVTVP 

       430        440 
VEVSRKNPKF METVAEKALQ EYRKKHREE

P10909 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools