SDC1_HUMAN
ID SDC1_HUMAN Reviewed; 310 AA.
AC P18827; D6W523; Q53QV0; Q546D3; Q96HB7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Syndecan-1;
DE Short=SYND1;
DE AltName: CD_antigen=CD138;
DE Flags: Precursor;
GN Name=SDC1; Synonyms=SDC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-136.
RC TISSUE=Fibroblast;
RX PubMed=1339431; DOI=10.1016/s0021-9258(18)48404-9;
RA Lories V., Cassiman J.-J., van de Berghe H., David G.;
RT "Differential expression of cell surface heparan sulfate proteoglycans in
RT human mammary epithelial cells and lung fibroblasts.";
RL J. Biol. Chem. 267:1116-1122(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-136.
RC TISSUE=Mammary gland;
RX PubMed=2324102; DOI=10.1016/s0021-9258(19)39232-4;
RA Mali M., Jaakkola P., Arvilommi A.-M., Jalkanen M.;
RT "Sequence of human syndecan indicates a novel gene family of integral
RT membrane proteoglycans.";
RL J. Biol. Chem. 265:6884-6889(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-136.
RX PubMed=15177497; DOI=10.1016/j.ejca.2004.01.038;
RA Mennerich D., Vogel A., Klaman I., Dahl E., Lichtner R.B., Rosenthal A.,
RA Pohlenz H.D., Thierauch K.H., Sommer A.;
RT "Shift of syndecan-1 expression from epithelial to stromal cells during
RT progression of solid tumours.";
RL Eur. J. Cancer 40:1373-1382(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-136.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-136.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-310, AND VARIANT GLN-136.
RC TISSUE=Placenta;
RX PubMed=9050911; DOI=10.1007/s004390050360;
RA Kaukonen J., Alanen-Kurki L., Jalkanen M., Palotie A.;
RT "The mapping and visual ordering of the human syndecan-1 and N-myc genes
RT near the telomeric region of chromosome 2p.";
RL Hum. Genet. 99:295-297(1997).
RN [8]
RP SHEDDING, AND SUBCELLULAR LOCATION.
RX PubMed=9169435; DOI=10.1074/jbc.272.23.14713;
RA Subramanian S.V., Fitzgerald M.L., Bernfield M.;
RT "Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth
RT factor receptor activation.";
RL J. Biol. Chem. 272:14713-14720(1997).
RN [9]
RP INTERACTION WITH CDCP1.
RX PubMed=16007225; DOI=10.1038/sj.onc.1208582;
RA Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.;
RT "Adhesion signaling by a novel mitotic substrate of src kinases.";
RL Oncogene 24:5333-5343(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 303-310 IN COMPLEX WITH TIAM1,
RP AND INTERACTION WITH TIAM1.
RX PubMed=23395182; DOI=10.1016/j.str.2013.01.004;
RA Liu X., Shepherd T.R., Murray A.M., Xu Z., Fuentes E.J.;
RT "The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a
RT ligand conformation that modulates protein dynamics.";
RL Structure 21:342-354(2013).
CC -!- FUNCTION: Cell surface proteoglycan that bears both heparan sulfate and
CC chondroitin sulfate and that links the cytoskeleton to the interstitial
CC matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP
CC (PubMed:22660413). {ECO:0000269|PubMed:22660413}.
CC -!- SUBUNIT: Interacts with CDCP1. Interacts (via C-terminus) with TIAM1
CC (via PDZ domain). Interacts with MDK (By similarity).
CC {ECO:0000250|UniProtKB:P26260, ECO:0000269|PubMed:16007225,
CC ECO:0000269|PubMed:23395182}.
CC -!- INTERACTION:
CC P18827; P05067: APP; NbExp=3; IntAct=EBI-2855248, EBI-77613;
CC P18827; P18827: SDC1; NbExp=2; IntAct=EBI-2855248, EBI-2855248;
CC P18827; P34741: SDC2; NbExp=2; IntAct=EBI-2855248, EBI-1172957;
CC P18827; Q13009: TIAM1; NbExp=5; IntAct=EBI-2855248, EBI-1050007;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:9169435}.
CC Secreted, extracellular exosome {ECO:0000269|PubMed:22660413}.
CC Note=Shedding of the ectodomain produces a soluble form.
CC {ECO:0000269|PubMed:9169435}.
CC -!- PTM: Shedding is enhanced by a number of factors such as heparanase,
CC thrombin or EGF. Also by stress and wound healing. PMA-mediated
CC shedding is inhibited by TIMP3. {ECO:0000269|PubMed:9169435}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SDC1ID42223ch2p24.html";
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DR EMBL; X60306; CAA42851.1; -; mRNA.
DR EMBL; J05392; AAA60605.1; -; mRNA.
DR EMBL; AJ551176; CAD80245.1; -; mRNA.
DR EMBL; AC104792; AAX93151.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00828.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00829.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00830.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00831.1; -; Genomic_DNA.
DR EMBL; BC008765; AAH08765.1; -; mRNA.
DR EMBL; Z48199; CAA88235.1; -; Genomic_DNA.
DR CCDS; CCDS1697.1; -.
DR PIR; A41776; A41776.
DR RefSeq; NP_001006947.1; NM_001006946.1.
DR RefSeq; NP_002988.3; NM_002997.4.
DR PDB; 4GVC; X-ray; 1.54 A; B=303-310.
DR PDB; 4GVD; X-ray; 1.85 A; C/D=303-310.
DR PDB; 6EJE; X-ray; 2.43 A; B=201-212.
DR PDBsum; 4GVC; -.
DR PDBsum; 4GVD; -.
DR PDBsum; 6EJE; -.
DR AlphaFoldDB; P18827; -.
DR SASBDB; P18827; -.
DR SMR; P18827; -.
DR BioGRID; 112284; 96.
DR ComplexPortal; CPX-3282; Syndecan-1-syntenin-1-ALIX complex.
DR CORUM; P18827; -.
DR DIP; DIP-1123N; -.
DR ELM; P18827; -.
DR IntAct; P18827; 50.
DR MINT; P18827; -.
DR STRING; 9606.ENSP00000370542; -.
DR ChEMBL; CHEMBL3712898; -.
DR TCDB; 9.A.35.1.2; the peptide translocating syndecan (syndecan) family.
DR GlyGen; P18827; 20 sites, 7 O-linked glycans (15 sites).
DR iPTMnet; P18827; -.
DR PhosphoSitePlus; P18827; -.
DR SwissPalm; P18827; -.
DR BioMuta; SDC1; -.
DR DMDM; 229463011; -.
DR EPD; P18827; -.
DR jPOST; P18827; -.
DR MassIVE; P18827; -.
DR MaxQB; P18827; -.
DR PaxDb; P18827; -.
DR PeptideAtlas; P18827; -.
DR PRIDE; P18827; -.
DR ProteomicsDB; 53609; -.
DR ABCD; P18827; 5 sequenced antibodies.
DR Antibodypedia; 1489; 1530 antibodies from 51 providers.
DR DNASU; 6382; -.
DR Ensembl; ENST00000254351.9; ENSP00000254351.4; ENSG00000115884.11.
DR Ensembl; ENST00000381150.5; ENSP00000370542.1; ENSG00000115884.11.
DR GeneID; 6382; -.
DR KEGG; hsa:6382; -.
DR MANE-Select; ENST00000254351.9; ENSP00000254351.4; NM_002997.5; NP_002988.4.
DR UCSC; uc002rdo.2; human.
DR CTD; 6382; -.
DR DisGeNET; 6382; -.
DR GeneCards; SDC1; -.
DR HGNC; HGNC:10658; SDC1.
DR HPA; ENSG00000115884; Tissue enhanced (esophagus, liver, skin).
DR MIM; 186355; gene.
DR neXtProt; NX_P18827; -.
DR OpenTargets; ENSG00000115884; -.
DR PharmGKB; PA35588; -.
DR VEuPathDB; HostDB:ENSG00000115884; -.
DR eggNOG; ENOG502RZWT; Eukaryota.
DR GeneTree; ENSGT00940000161171; -.
DR HOGENOM; CLU_887201_0_0_1; -.
DR InParanoid; P18827; -.
DR OMA; QPAMPQI; -.
DR OrthoDB; 1340825at2759; -.
DR PhylomeDB; P18827; -.
DR TreeFam; TF320463; -.
DR PathwayCommons; P18827; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR Reactome; R-HSA-2024096; HS-GAG degradation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
DR Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P18827; -.
DR BioGRID-ORCS; 6382; 266 hits in 1071 CRISPR screens.
DR ChiTaRS; SDC1; human.
DR GeneWiki; Syndecan_1; -.
DR GenomeRNAi; 6382; -.
DR Pharos; P18827; Tbio.
DR PRO; PR:P18827; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P18827; protein.
DR Bgee; ENSG00000115884; Expressed in lower esophagus mucosa and 163 other tissues.
DR ExpressionAtlas; P18827; baseline and differential.
DR Genevisible; P18827; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0048627; P:myoblast development; ISS:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IMP:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0055002; P:striated muscle cell development; IEP:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR031190; Syndecan-1.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; PTHR10915; 1.
DR PANTHER; PTHR10915:SF5; PTHR10915:SF5; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein;
KW Proteoglycan; Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..310
FT /note="Syndecan-1"
FT /id="PRO_0000033499"
FT TOPO_DOM 23..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 27..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 242..243
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 37
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 206
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 216
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT VARIANT 76
FT /note="T -> M (in dbSNP:rs2230922)"
FT /id="VAR_052242"
FT VARIANT 136
FT /note="L -> Q (in dbSNP:rs10205485)"
FT /evidence="ECO:0000269|PubMed:1339431,
FT ECO:0000269|PubMed:15177497, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2324102, ECO:0000269|PubMed:9050911,
FT ECO:0000269|Ref.5"
FT /id="VAR_052243"
FT CONFLICT 19
FT /note="P -> L (in Ref. 2; AAA60605)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="G -> V (in Ref. 6; AAH08765)"
FT /evidence="ECO:0000305"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:4GVC"
SQ SEQUENCE 310 AA; 32462 MW; 8E9EF4A57F5FDBD0 CRC64;
MRRAALWLWL CALALSLQPA LPQIVATNLP PEDQDGSGDD SDNFSGSGAG ALQDITLSQQ
TPSTWKDTQL LTAIPTSPEP TGLEATAAST STLPAGEGPK EGEAVVLPEV EPGLTAREQE
ATPRPRETTQ LPTTHLASTT TATTAQEPAT SHPHRDMQPG HHETSTPAGP SQADLHTPHT
EDGGPSATER AAEDGASSQL PAAEGSGEQD FTFETSGENT AVVAVEPDRR NQSPVDQGAT
GASQGLLDRK EVLGGVIAGG LVGLIFAVCL VGFMLYRMKK KDEGSYSLEE PKQANGGAYQ
KPTKQEEFYA
