ID   SDC2_HUMAN              Reviewed;         201 AA.
AC   P34741; B3KQA3; Q6PIS6; Q9H6V1;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   24-JAN-2024, entry version 205.
DE   RecName: Full=Syndecan-2;
DE            Short=SYND2;
DE   AltName: Full=Fibroglycan;
DE   AltName: Full=Heparan sulfate proteoglycan core protein;
DE            Short=HSPG;
DE   AltName: CD_antigen=CD362;
DE   Flags: Precursor;
GN   Name=SDC2; Synonyms=HSPG1;
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 THR-71.
RC   TISSUE=Lung fibroblast;
RX   PubMed=2523388; DOI=10.1016/s0021-9258(18)83534-7;
RA   Marynen P., Zhang J., Cassiman J.-J., den Berghe H., David G.;
RT   "Partial primary structure of the 48- and 90-kilodalton core proteins of
RT   cell surface-associated heparan sulfate proteoglycans of lung fibroblasts.
RT   Prediction of an integral membrane domain and evidence for multiple
RT   distinct core proteins at the cell surface of human lung fibroblasts.";
RL   J. Biol. Chem. 264:7017-7024(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-59.
RC   TISSUE=Embryo;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-71.
RC   TISSUE=Brain, and Muscle;
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   GLYCOSYLATION AT THR-101, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT   O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [9]
RP   IDENTIFICATION IN A COMPLEX WITH SDCBP AND PDCD6IP.
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   [10]
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   [11]
RP   PHOSPHORYLATION AT SER-115.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
CC   -!- FUNCTION: Cell surface proteoglycan which regulates dendritic arbor
CC       morphogenesis. {ECO:0000250|UniProtKB:P43407}.
CC   -!- SUBUNIT: Interacts (via cytoplasmic domain) with SARM1 (By similarity).
CC       Forms a complex with SDCBP and PDCD6IP (PubMed:22660413).
CC       {ECO:0000250|UniProtKB:P43407, ECO:0000269|PubMed:22660413}.
CC   -!- INTERACTION:
CC       P34741; Q12797-6: ASPH; NbExp=5; IntAct=EBI-1172957, EBI-12092171;
CC       P34741; O14936: CASK; NbExp=2; IntAct=EBI-1172957, EBI-1215506;
CC       P34741; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1172957, EBI-10976677;
CC       P34741; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-1172957, EBI-10213520;
CC       P34741; O15354: GPR37; NbExp=3; IntAct=EBI-1172957, EBI-15639515;
CC       P34741; P28799: GRN; NbExp=3; IntAct=EBI-1172957, EBI-747754;
CC       P34741; P28799-2: GRN; NbExp=3; IntAct=EBI-1172957, EBI-25860013;
CC       P34741; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1172957, EBI-10975473;
CC       P34741; Q13387-4: MAPK8IP2; NbExp=3; IntAct=EBI-1172957, EBI-12345753;
CC       P34741; P41271-2: NBL1; NbExp=3; IntAct=EBI-1172957, EBI-12135485;
CC       P34741; P21359: NF1; NbExp=4; IntAct=EBI-1172957, EBI-1172917;
CC       P34741; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-1172957, EBI-9090282;
CC       P34741; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1172957, EBI-396669;
CC       P34741; P18827: SDC1; NbExp=2; IntAct=EBI-1172957, EBI-2855248;
CC       P34741; P34741: SDC2; NbExp=4; IntAct=EBI-1172957, EBI-1172957;
CC       P34741; O75056: SDC3; NbExp=2; IntAct=EBI-1172957, EBI-1642090;
CC       P34741; P31431: SDC4; NbExp=2; IntAct=EBI-1172957, EBI-3913237;
CC       P34741; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1172957, EBI-5235340;
CC       P34741; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-1172957, EBI-11123832;
CC       P34741; O60784-2: TOM1; NbExp=3; IntAct=EBI-1172957, EBI-12117154;
CC       P34741; O76024: WFS1; NbExp=3; IntAct=EBI-1172957, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans. Contains
CC       heparan sulfate (PubMed:22171320). Also contains chondroitin sulfate
CC       (By similarity). {ECO:0000250|UniProtKB:P43407,
CC       ECO:0000269|PubMed:22171320}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA52701.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; J04621; AAA52701.1; ALT_INIT; mRNA.
DR   EMBL; AK025488; BAB15150.1; -; mRNA.
DR   EMBL; AK074530; BAG51965.1; -; mRNA.
DR   EMBL; AK097839; BAG53540.1; -; mRNA.
DR   EMBL; CH471060; EAW91755.1; -; Genomic_DNA.
DR   EMBL; BC030133; AAH30133.1; -; mRNA.
DR   EMBL; BC049836; AAH49836.1; -; mRNA.
DR   CCDS; CCDS6272.1; -.
DR   PIR; A33880; A33880.
DR   RefSeq; NP_002989.2; NM_002998.3.
DR   PDB; 6ITH; NMR; -; A=143-173.
DR   PDBsum; 6ITH; -.
DR   AlphaFoldDB; P34741; -.
DR   SASBDB; P34741; -.
DR   SMR; P34741; -.
DR   BioGRID; 112285; 141.
DR   CORUM; P34741; -.
DR   DIP; DIP-29943N; -.
DR   IntAct; P34741; 89.
DR   MINT; P34741; -.
DR   STRING; 9606.ENSP00000307046; -.
DR   BindingDB; P34741; -.
DR   ChEMBL; CHEMBL4888448; -.
DR   DrugBank; DB00020; Sargramostim.
DR   GlyConnect; 707; 1 O-Linked glycan (1 site).
DR   GlyCosmos; P34741; 5 sites, 4 glycans.
DR   GlyGen; P34741; 11 sites, 5 O-linked glycans (8 sites).
DR   iPTMnet; P34741; -.
DR   PhosphoSitePlus; P34741; -.
DR   BioMuta; SDC2; -.
DR   DMDM; 158962336; -.
DR   EPD; P34741; -.
DR   jPOST; P34741; -.
DR   MassIVE; P34741; -.
DR   PaxDb; 9606-ENSP00000307046; -.
DR   PeptideAtlas; P34741; -.
DR   ProteomicsDB; 54941; -.
DR   Pumba; P34741; -.
DR   Antibodypedia; 25987; 311 antibodies from 31 providers.
DR   DNASU; 6383; -.
DR   Ensembl; ENST00000302190.9; ENSP00000307046.4; ENSG00000169439.12.
DR   GeneID; 6383; -.
DR   KEGG; hsa:6383; -.
DR   MANE-Select; ENST00000302190.9; ENSP00000307046.4; NM_002998.4; NP_002989.2.
DR   UCSC; uc003yhv.2; human.
DR   AGR; HGNC:10659; -.
DR   CTD; 6383; -.
DR   DisGeNET; 6383; -.
DR   GeneCards; SDC2; -.
DR   HGNC; HGNC:10659; SDC2.
DR   HPA; ENSG00000169439; Tissue enhanced (liver, thyroid gland).
DR   MIM; 142460; gene.
DR   neXtProt; NX_P34741; -.
DR   OpenTargets; ENSG00000169439; -.
DR   PharmGKB; PA35589; -.
DR   VEuPathDB; HostDB:ENSG00000169439; -.
DR   eggNOG; ENOG502RZ6V; Eukaryota.
DR   GeneTree; ENSGT00940000157222; -.
DR   HOGENOM; CLU_046599_2_1_1; -.
DR   InParanoid; P34741; -.
DR   OMA; ASASGSX; -.
DR   OrthoDB; 4258425at2759; -.
DR   PhylomeDB; P34741; -.
DR   TreeFam; TF320463; -.
DR   PathwayCommons; P34741; -.
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-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-HSA-9694614; Attachment and Entry.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SignaLink; P34741; -.
DR   SIGNOR; P34741; -.
DR   BioGRID-ORCS; 6383; 8 hits in 1151 CRISPR screens.
DR   ChiTaRS; SDC2; human.
DR   GeneWiki; SDC2; -.
DR   GenomeRNAi; 6383; -.
DR   Pharos; P34741; Tbio.
DR   PRO; PR:P34741; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P34741; Protein.
DR   Bgee; ENSG00000169439; Expressed in tibia and 207 other cell types or tissues.
DR   ExpressionAtlas; P34741; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:BHF-UCL.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0048813; P:dendrite morphogenesis; IBA:GO_Central.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR001050; Syndecan.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   InterPro; IPR030479; Syndecan_CS.
DR   PANTHER; PTHR10915; SYNDECAN; 1.
DR   PANTHER; PTHR10915:SF6; SYNDECAN-2; 1.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   PROSITE; PS00964; SYNDECAN; 1.
DR   Genevisible; P34741; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Differentiation; Glycoprotein; Heparan sulfate; Membrane;
KW   Neurogenesis; Phosphoprotein; Proteoglycan; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..201
FT                   /note="Syndecan-2"
FT                   /id="PRO_0000033503"
FT   TOPO_DOM        19..144
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          42..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            142..143
FT                   /note="Cleavage of ectodomain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         115
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CARBOHYD        41
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        55
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:22171320"
FT   VARIANT         59
FT                   /note="A -> T (in dbSNP:rs3816208)"
FT                   /evidence="ECO:0000269|PubMed:16303743"
FT                   /id="VAR_034675"
FT   VARIANT         71
FT                   /note="S -> T (in dbSNP:rs1042381)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2523388"
FT                   /id="VAR_034676"
FT   CONFLICT        150
FT                   /note="I -> T (in Ref. 2; BAB15150)"
FT                   /evidence="ECO:0000305"
FT   HELIX           143..171
FT                   /evidence="ECO:0007829|PDB:6ITH"
SQ   SEQUENCE   201 AA;  22160 MW;  7DA4159D54741054 CRC64;
     MRRAWILLTL GLVACVSAES RAELTSDKDM YLDNSSIEEA SGVYPIDDDD YASASGSGAD
     EDVESPELTT SRPLPKILLT SAAPKVETTT LNIQNKIPAQ TKSPEETDKE KVHLSDSERK
     MDPAEEDTNV YTEKHSDSLF KRTEVLAAVI AGGVIGFLFA IFLILLLVYR MRKKDEGSYD
     LGERKPSSAA YQKAPTKEFY A
//