ID A0A452IKY1_9SAUR Unreviewed; 309 AA.
AC A0A452IKY1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Syndecan {ECO:0000256|RuleBase:RU000649};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000028568.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000028568.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Cell surface proteoglycan. {ECO:0000256|RuleBase:RU000649}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU000649}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000649}.
CC Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family.
CC {ECO:0000256|ARBA:ARBA00005343, ECO:0000256|RuleBase:RU000649}.
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DR AlphaFoldDB; A0A452IKY1; -.
DR STRING; 38772.ENSGAGP00000028568; -.
DR Ensembl; ENSGAGT00000032445.1; ENSGAGP00000028568.1; ENSGAGG00000020696.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF5; SYNDECAN-1; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU000649};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207,
KW ECO:0000256|RuleBase:RU000649};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974,
KW ECO:0000256|RuleBase:RU000649};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000649};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..309
FT /note="Syndecan"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019405953"
FT TRANSMEM 252..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..293
FT /note="Neurexin/syndecan/glycophorin C"
FT /evidence="ECO:0000259|SMART:SM00294"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 32909 MW; 98469DFDA1767BD6 CRC64;
MINVSAVWLL ALFLQAACSQ TTNLNLPPED QDSSGDDEDA FSGSGAGPLT DHPVVALNIP
LEHANSSTMS TGATVHQPAV HGTENPAEKE TVSSPTSDVV PDEAVLSDKD EIHKLRSAAE
KPTTSEAILT RSPTTHSPTV RVTTAQASST VHVTEPSIHS SSSSGVSKET LDPNFTTISE
EDVHFPTTTI LPRGVYPIDE KEIPFPEESS GDQGDFIFSE EGTIPSESEL ADSSRDAEAA
GTSQGLMDRK EVLGGVIAGG LVGLLFAVFL VGFMLYRMKK KDEGSYSLDE PKQSNGGYQK
PQKQEEFYA
//