ID A0A1S3RWT6_SALSA Unreviewed; 1017 AA.
AC A0A1S3RWT6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Platelet endothelial aggregation receptor 1-like isoform X2 {ECO:0000313|RefSeq:XP_014056264.1};
GN Name=LOC106605310 {ECO:0000313|RefSeq:XP_014056264.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014056264.1};
RN [1] {ECO:0000313|RefSeq:XP_014056264.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014056264.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014056264.1; XM_014200789.1.
DR AlphaFoldDB; A0A1S3RWT6; -.
DR STRING; 8030.ENSSSAP00000020225; -.
DR PaxDb; 8030-ENSSSAP00000020225; -.
DR Ensembl; ENSSSAT00000205728; ENSSSAP00000175603; ENSSSAG00000009866.
DR GeneID; 106605310; -.
DR OMA; VCHNGAK; -.
DR OrthoDB; 2540323at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR Bgee; ENSSSAG00000009866; Expressed in muscle tissue and 11 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 4.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24052; DELTA-RELATED; 1.
DR PANTHER; PTHR24052:SF12; PLATELET ENDOTHELIAL AGGREGATION RECEPTOR 1; 1.
DR Pfam; PF00053; Laminin_EGF; 4.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00180; EGF_Lam; 12.
DR PROSITE; PS00022; EGF_1; 12.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS51041; EMI; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|RefSeq:XP_014056264.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1017
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010237471"
FT TRANSMEM 752..775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..104
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 146..176
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 223..257
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 270..300
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 308..343
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 402..432
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 483..518
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 569..604
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 612..648
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 656..691
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 914..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 166..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 247..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 290..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 333..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 422..431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 508..517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 594..603
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 638..647
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 681..690
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1017 AA; 110516 MW; 54809D4970A778AC CRC64;
MQSLQTCSVL LVLSVLIGLS WSLNPRDPNV CSLWESFTTS VKESYAHPYD QVTEEPCSEP
RTSYRCTRHR ITYKTAYRQA VKMDYRRRYQ CCPGYYESRD KCVPRCTKEC VHGRCVAPDR
CQCEGGWRGD DCSSACDDKH WGPGCGQLCK CENGGLCNPV TGTCQCPPGY IGRRCEDPCP
PGTFGKGCLQ KCQCGTGGSC DKVTGECLCR EHFTGTFCEK ACPKSPCPLR CPCQNGGICQ
GKGICACPPG WTGEVCTERC TEGRFGPNCA HECVCHNRGH CDPETGHCQC AEGFTGNRCS
EECQVGSYGR DCKGVCDCAN GSRCYNIDGG CLCEPGFSGP QCRERMCRHG TYGLQCERTC
LCHDTHTLSC HPLKGECTCQ PGWAGLYCNE TCARGYYGHG CLEPCLCVNG GVCDSVSGRC
HCAPGYTGVH CESPCKSGTY GKNCSLECSC SNSVDCSPID GTCFCKEGWR GRYCSIPCSK
GTWGPGCNAT CQCANGALCN PADGSCTCSP GWKGPLCDQP CPMGTFGPGC LKRCDCLNAD
GCQGASGQCQ CLPGWTGARC AQTCPEGTWG RHCNQSCFCQ NSATCLPHSG ACVCLPGYWG
PTCQHMCSAG VYGDQCSITC PSCAHSSSCH HVTGQCVCKP GYTGALCEQA CPVGLYGKQC
TGVCRCAHNS SCHHQDGSCL CPPGWTGPDC TLQCHHGMFG LNCAQVCSCP PNFYCDPQTG
ECVCESGPGI DCKKERFVSM MVPVSPGERD SWGAIAGIVV LVMLVVLLLA LLLLYRRRQK
DKQANTPTVS FSTSRTVNSE YAIPDVPHNY HHYYNHSYHT LTGSRPPLPH VPNNQDRAIK
NTNNQLFCDV KNMERERGLF GVESNATLPA DWKHHEARKE PGAFSIDRSY SYSASLGKYY
NKVTELKDTG VAASSSSLNS ENPYATIKDL PGLPFGPPES SYMEMRTAMP HERSYTEISP
PPFSTSTLRR ERSSLGRVPE QEPHNHYDLP VNSHIPGHYD LPPVRRPPSP VRRRLPQ
//
