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UniProtKB/Swiss-Prot entry P02511


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CRYAB_HUMAN
Primary accession number P02511
Secondary accession numbers B0YIX0 O43416 Q9UC37 Q9UC38 Q9UC39 Q9UC40 Q9UC41
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 1, 1990 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 115)
Name and origin of the protein
Protein name Alpha-crystallin B chain
Synonyms Alpha(B)-crystallin
Rosenthal fiber component
Heat shock protein beta-5
HspB5
Renal carcinoma antigen NY-REN-27
Gene name
Name: CRYAB
Synonyms: CRYA2
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]
PRELIMINARY PROTEIN SEQUENCE.
DOI=10.1016/0014-5793(77)80757-6; PubMed=838078 [NCBI, ExPASy, EBI, Israel, Japan]
Kramps J.A., de Man B.M., de Jong W.W.;
"The primary structure of the B2 chain of human alpha-crystallin.";
FEBS Lett. 74:82-84(1977).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(90)90204-8; PubMed=2387586 [NCBI, ExPASy, EBI, Israel, Japan]
Dubin R.A., Ally A.H., Chung S., Piatigorsky J.;
"Human alpha B-crystallin gene and preferential promoter function in lens.";
Genomics 7:594-601(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0304-3940(92)90689-5; PubMed=1407707 [NCBI, ExPASy, EBI, Israel, Japan]
Iwaki A., Iwaki T., Goldman J.E., Ogomori K., Tateishi J., Sakaki Y.;
"Accumulation of alpha B-crystallin in brains of patients with Alexander's disease is not due to an abnormality of the 5'-flanking and coding sequence of the genomic DNA.";
Neurosci. Lett. 140:89-92(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Yu W., Sarginson J., Gibbs R.A.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
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]
PROTEIN SEQUENCE OF 2-24; 35-66 AND 118-175, AND ASSOCIATION WITH HSPB1.
TISSUE=Pectoralis muscle;
PubMed=1560006 [NCBI, ExPASy, EBI, Israel, Japan]
Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.;
"Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle.";
J. Biol. Chem. 267:7718-7725(1992).
[11]
PROTEIN SEQUENCE OF 57-66.
DOI=10.1074/jbc.272.4.2268; PubMed=8999933 [NCBI, ExPASy, EBI, Israel, Japan]
Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L.;
"Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens.";
J. Biol. Chem. 272:2268-2275(1997).
[12]
PROTEIN SEQUENCE OF 83-89 AND 164-172.
TISSUE=Heart;
DOI=10.1002/elps.11501601192; PubMed=7498159 [NCBI, ExPASy, EBI, Israel, Japan]
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein database of human heart.";
Electrophoresis 16:1160-1169(1995).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 107-175.
DOI=10.1016/0092-8674(89)90173-6; PubMed=2539261 [NCBI, ExPASy, EBI, Israel, Japan]
Iwaki T., Kume-Iwaki A., Liem R.K.H., Goldman J.E.;
"Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain.";
Cell 57:71-78(1989).
[14]
RACEMIZATION/ISOMERIZATION OF SPECIFIC ASP.
DOI=10.1016/0167-4838(94)90003-5; PubMed=8142454 [NCBI, ExPASy, EBI, Israel, Japan]
Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K.;
"Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens.";
Biochim. Biophys. Acta 1204:157-163(1994).
[15]
PHOSPHORYLATION AT SER-19; SER-45 AND SER-59, AND MASS SPECTROMETRY.
PubMed=8175657 [NCBI, ExPASy, EBI, Israel, Japan]
Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., Smith J.B.;
"Post-translational modifications of water-soluble human lens crystallins from young adults.";
J. Biol. Chem. 269:12494-12502(1994).
[16]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; PubMed=10508479 [NCBI, ExPASy, EBI, Israel, Japan]
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[17]
MASS SPECTROMETRY, SUSCEPTIBILITY TO OXIDATION, AND PHOSPHORYLATION.
DOI=10.1006/exer.2000.0868; PubMed=10930324 [NCBI, ExPASy, EBI, Israel, Japan]
Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.;
"The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage.";
Exp. Eye Res. 71:195-207(2000).
[18]
INTERACTION WITH HSPBAP1.
DOI=10.1074/jbc.M001981200; PubMed=10751411 [NCBI, ExPASy, EBI, Israel, Japan]
Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
"Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27.";
J. Biol. Chem. 275:18724-18731(2000).
[19]
PHOSPHORYLATION AT SER-45 AND SER-59.
DOI=10.1046/j.1471-4159.2001.00038.x; PubMed=11158243 [NCBI, ExPASy, EBI, Israel, Japan]
Kato K., Inaguma Y., Ito H., Iida K., Iwamoto I., Kamei K., Ochi N., Ohta H., Kishikawa M.;
"Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease.";
J. Neurochem. 76:730-736(2001).
[20]
ACETYLATION AT LYS-92.
DOI=10.1110/ps.40901; PubMed=11369851 [NCBI, ExPASy, EBI, Israel, Japan]
Lapko V.N., Smith D.L., Smith J.B.;
"In vivo carbamylation and acetylation of water-soluble human lens alphaB-crystallin lysine 92.";
Protein Sci. 10:1130-1136(2001).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; SER-43; SER-45; SER-53; SER-59 AND SER-76, METHYLATION AT ARG-22 AND ARG-50, ACETYLATION AT LYS-92, SUSCEPTIBILITY TO OXIDATION, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.122231399; PubMed=12060738 [NCBI, ExPASy, EBI, Israel, Japan]
MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M., Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I., Yates J.R. III;
"Shotgun identification of protein modifications from protein complexes and lens tissue.";
Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002).
[22]
INVOLVEMENT IN ALPHA-B CRYSTALLINOPATHY.
DOI=10.1002/ana.10767; PubMed=14681890 [NCBI, ExPASy, EBI, Israel, Japan]
Selcen D., Engel A.G.;
"Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations.";
Ann. Neurol. 54:804-810(2003).
[23]
INTERACTION WITH TTN.
DOI=10.1074/jbc.M307473200; PubMed=14676215 [NCBI, ExPASy, EBI, Israel, Japan]
Bullard B., Ferguson C., Minajeva A., Leake M.C., Gautel M., Labeit D., Ding L., Labeit S., Horwitz J., Leonard K.R., Linke W.A.;
"Association of the chaperone alphaB-crystallin with titin in heart muscle.";
J. Biol. Chem. 279:7917-7924(2004).
[24]
VARIANT ALPHA-B CRYSTALLINOPATHY GLY-120.
DOI=10.1038/1765; PubMed=9731540 [NCBI, ExPASy, EBI, Israel, Japan]
Vicart P., Caron A., Guicheney P., Li Z., Prevost M.-C., Faure A., Chateau D., Chapon F., Tome F., Dupret J.-M., Paulin D., Fardeau M.;
"A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy.";
Nat. Genet. 20:92-95(1998).
[25]
CHARACTERIZATION OF VARIANTS ALPHA-B CRYSTALLINOPATHY GLY-120.
DOI=10.1167/iovs.02-0950; PubMed=12601044 [NCBI, ExPASy, EBI, Israel, Japan]
Fu L., Liang J.J.-N.;
"Alteration of protein-protein interactions of congenital cataract crystallin mutants.";
Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003).
Comments
  • FUNCTION: May contribute to the transparency and refractive index of the lens.
  • SUBUNIT: Aggregates with homologous proteins, including CRYAA and the small heat shock protein HSPB1, to form large heteromeric complexes. Interacts with HSPBAP1 and TTN/titin.
  • INTERACTION:
    Q9UJY1:HSPB8; NbExp=1; IntAct=EBI-739060, EBI-739074;
  • TISSUE SPECIFICITY: Lens as well as other tissues.
  • MASS SPECTROMETRY: Mass=20201; Method=Electrospray; Range=1-175; Source=PubMed:8175657;.
  • MASS SPECTROMETRY: Mass=20281; Method=Electrospray; Range=1-175; Note=With 1 phosphate group; Source=PubMed:8175657;.
  • MASS SPECTROMETRY: Mass=20360; Method=Electrospray; Range=1-175; Note=With 2 phosphate groups; Source=PubMed:8175657;.
  • MASS SPECTROMETRY: Mass=20199; Method=Electrospray; Range=1-175; Source=PubMed:10930324;.
  • MASS SPECTROMETRY: Mass=20278; Method=Electrospray; Range=1-175; Note=With 1 phosphate group; Source=PubMed:10930324;.
  • DISEASE: Seen as Rosenthal fiber protein in the brain tissue of patients with Alexander disease.
  • DISEASE: Defects in CRYAB are the cause of alpha-B crystallinopathy [MIM:608810]. Alpha-B crystallinopathy is a an autosomal dominant form of desmin-related myopathy (DRM) that results in weakness of the proximal and distal limb muscle (including neck, velopharynx, and trunk muscles), signs of cardiomyopathy and cataract. Patients with progressive myopathy characterized by myofibrillar degeneration that commences at the Z-disk, have been described. Mutations truncate the essential C-terminal domain of the protein required for the chaperone function.
  • DISEASE: Crystallins do not turn over as the lens ages, providing ample opportunity for post-translational modifications or oxidations. These modifications may change crystallin solubility properties and favor senile cataract.
  • SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=CRYAB";.
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
M28638; AAA52104.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S45630; AAB23453.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF007162; AAC19161.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314029; BAG36739.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006770; AAP35416.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
EF444955; ACA05949.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471065; EAW67162.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007008; AAH07008.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24906; AAA60267.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00021369; -.
PIR A35332; CYHUAB.
RefSeq NP_001876.1; -.
UniGene Hs.408767
3D structure databases
DisProt DP00445; -.
ModBase P02511.
Protein-protein interaction databases
IntAct P02511; 2.
PTM databases
GlycoSuiteDB P02511; -.
PhosphoSite P02511; -.
2D gel databases
SWISS-2DPAGE P02511; -.
HSC-2DPAGE P02511; -.
REPRODUCTION-2DPAGE IPI00021369; -.
Organism-specific databases
GeneCards GC11M111284; -.
H-InvDB HIX0010115; -.
HGNC HGNC:2389; CRYAB.
GenAtlas CRYAB.
HPA CAB002053; -.
MIM 123590; gene+phenotype. [NCBI / EBI]
608810; phenotype. [NCBI / EBI]
Orphanet 98993; Cataract, posterior polar.
98995; Cataract, zonular.
593; Myofibrillary myopathy.
91492; Non-syndromic congenital cataract.
PharmGKB PA26907; -.
Gene expression databases
ArrayExpress P02511; -.
Bgee P02511; -.
CleanEx HS_CRYAB; -.
GermOnline ENSG00000109846; Homo sapiens.
Ontologies
GO
GO:0005212; Molecular function: structural constituent of eye lens (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (inferred from physical interaction from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from direct assay from HGNC).
GO:0006936; Biological process: muscle contraction (traceable author statement from ProtInc).
GO:0032387; Biological process: negative regulation of intracellular transport (inferred from direct assay from HGNC).
GO:0006457; Biological process: protein folding (non-traceable author statement from ProtInc).
GO:0051260; Biological process: protein homooligomerization (inferred from direct assay from UniProtKB).
GO:0009408; Biological process: response to heat (inferred from electronic annotation from InterPro).
GO:0007169; Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001436; Alpha-crystallin/HSP.
IPR012273; Alpha-crystallin_B.
IPR003090; Alpha-crystallin_N.
IPR002068; Hsp20.
Graphical view of domain structure.
PANTHER PTHR11527:SF37; A-crystallin_B; 1.
Pfam PF00525; Crystallin; 1.
PF00011; HSP20; 1.
Pfam graphical view of domain structure.
PRINTS PR00299; ACRYSTALLIN.
ProDom PD001193; Crystallin_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS01031; HSP20; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P02511; -.
Genome annotation databases
Ensembl ENSG00000109846; Homo sapiens. [Contig view]
GeneID 1410; -.
KEGG hsa:1410; -.
Phylogenomic databases
HOGENOM P02511; -.
HOVERGEN P02511; -.
OMA P02511; DRYVIYL.
Other
NextBio 5765; -.
PMAP-CutDB P02511; -.
SOURCE CRYAB; Homo sapiens.
ProtoNet P02511.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cataract; Desmin-related myopathy; Direct protein sequencing; Disease mutation; Eye lens protein; Glycoprotein; Methylation; Oxidation; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   175  175     Alpha-crystallin B chain. PRO_0000125907
SITE   48    48  1     Susceptible to oxidation. 
SITE   60    60  1     Susceptible to oxidation. 
SITE   68    68  1     Susceptible to oxidation. 
MOD_RES   1     1        N-acetylmethionine (Probable). 
MOD_RES   19    19        Phosphoserine. 
MOD_RES   21    21        Phosphoserine. 
MOD_RES   22    22        Omega-N-methylated arginine. 
MOD_RES   43    43        Phosphoserine. 
MOD_RES   45    45        Phosphoserine. 
MOD_RES   50    50        Omega-N-methylated arginine. 
MOD_RES   53    53        Phosphoserine. 
MOD_RES   59    59        Phosphoserine. 
MOD_RES   76    76        Phosphoserine. 
MOD_RES   92    92        N6-acetyllysine; partial. 
CARBOHYD   170   170        O-linked (GlcNAc) (By similarity). 
VARIANT   41    41  1     S -> Y (in dbSNP:rs2234703 [NCBI]). VAR_014607 
VARIANT   51    51  1     P -> L (in dbSNP:rs2234704 [NCBI]). VAR_014608 
VARIANT   120   120  1     R -> G (in alpha-B crystallinopathy; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC). VAR_007899 
CONFLICT   165   165        E -> K (in Ref. 4; AAC19161). 
CONFLICT   175   175        K -> KKMPFLELHFLKQESFPTSE (in Ref. 4; AAC19161). 
Sequence information
Length: 175 AA [This is the length of the unprocessed precursor] Molecular weight: 20159 Da [This is the MW of the unprocessed precursor] CRC64: AE08BED46B7849CB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW 

        70         80         90        100        110        120 
FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 

       130        140        150        160        170 
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK 

P02511 in FASTA format

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