SDC1_BOVIN
ID SDC1_BOVIN Reviewed; 311 AA.
AC Q08DZ5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Syndecan-1;
DE Short=SYND1;
DE AltName: CD_antigen=CD138;
DE Flags: Precursor;
GN Name=SDC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250|UniProtKB:P18827}.
CC -!- SUBUNIT: Interacts with CDCP1. Interacts (via C-terminus) with TIAM1
CC (via PDZ domain) (By similarity). Interacts with MDK (By similarity).
CC {ECO:0000250|UniProtKB:P18827, ECO:0000250|UniProtKB:P26260}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Secreted
CC {ECO:0000250|UniProtKB:P18827}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P18827}. Note=Shedding of the ectodomain
CC produces a soluble form. {ECO:0000250|UniProtKB:P18827}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P18827}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; BC123495; AAI23496.1; -; mRNA.
DR RefSeq; NP_001069392.1; NM_001075924.1.
DR AlphaFoldDB; Q08DZ5; -.
DR STRING; 9913.ENSBTAP00000014810; -.
DR PaxDb; Q08DZ5; -.
DR PeptideAtlas; Q08DZ5; -.
DR Ensembl; ENSBTAT00000014810; ENSBTAP00000014810; ENSBTAG00000011154.
DR GeneID; 529759; -.
DR KEGG; bta:529759; -.
DR CTD; 6382; -.
DR VEuPathDB; HostDB:ENSBTAG00000011154; -.
DR VGNC; VGNC:34378; SDC1.
DR eggNOG; ENOG502RZWT; Eukaryota.
DR GeneTree; ENSGT00940000161171; -.
DR HOGENOM; CLU_887201_0_0_1; -.
DR InParanoid; Q08DZ5; -.
DR OMA; QPAMPQI; -.
DR OrthoDB; 1340825at2759; -.
DR TreeFam; TF320463; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000011154; Expressed in esophagus and 99 other tissues.
DR ExpressionAtlas; Q08DZ5; baseline.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IEA:InterPro.
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 2: Evidence at transcript level;
KW Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein; Proteoglycan;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..311
FT /note="Syndecan-1"
FT /id="PRO_0000290107"
FT TOPO_DOM 23..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 31..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 251..252
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18827"
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 204
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 214
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 311 AA; 32316 MW; 31E163B82F35BBC1 CRC64;
MRRAALWLWL CALALRLQPA LLHSVAVNMP PEDQDGSGDD SDNFSGSGAG ALPDITSSHT
PSTWKDLGPV TTTATAPEPT SPDAIAASTT ILPTGEQPEG GRAVLLAEVE PGLTAQKEAT
HPPSETTLHP TTHSVSTARA TMAPGPATSH PHRDVQPDHH ETSAPTGRGR MEPHRPHVEE
GGPPATEKAA EEDPSTQIPV GEGSGEQDFT FDLSGENAAG AAGEPGSRNG APEDPEATGA
TGASQGLLDR KEVLGGVIAG GLVGLIFAVC LVGFMLYRMK KKDEGSYSLE EPKQANGGAY
QKPTKQEEFY A
