ID A0A1S3NVE4_SALSA Unreviewed; 1381 AA.
AC A0A1S3NVE4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X3 {ECO:0000313|RefSeq:XP_014019359.1};
GN Name=LOC106581675 {ECO:0000313|RefSeq:XP_014019359.1};
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_014019359.1};
RN [1] {ECO:0000313|RefSeq:XP_014019359.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014019359.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014019359.1; XM_014163884.1.
DR Ensembl; ENSSSAT00000200726; ENSSSAP00000158507; ENSSSAG00000053453.
DR GeneID; 106581675; -.
DR OrthoDB; 5363002at2759; -.
DR Proteomes; UP000087266; Chromosome ssa21.
DR Bgee; ENSSSAG00000053453; Expressed in mesonephros and 13 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1081; COLLAGEN TYPE XVIII, ALPHA 1 ISOFORM X1; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_014019359.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1381
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010197227"
FT DOMAIN 30..219
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 221..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..856
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1381 AA; 142209 MW; 95FBEC311459C1FA CRC64;
MEMRCCSWPL LCFVLVLLTP VASQWPDEIG VSLLHLIGDP PPEEITKIYG PDNSPGYVFG
PDANTGQLAR AHLPSPFYRD FSLLFNLKPQ STKGGVIFSV TDASQKIMYV GVKLSPVKAS
KQNVIFYYTE PDSQVSYVAA TFPVHNLADQ WNRFSISVLD DKVTFYINCD DQPQVVRFER
SPDEMELEPG AGVFVGQAGG ADPDKFLGVI GELRVVGNPR AAERQCEEEG DDSDVASGDG
GSGDVEGKLD GKKKGPGTFK WDAEVQKYVW VEDDRPTVTT TPPSSRPIQQ PPVTRQQPEV
SPKKETGPGG SRGEKGDRGE KGDRGPFGPK GDSGSESGTR GGAHGEKGVP GEKGIKGKAG
FGYPGSKGDP GPAGPPGPPG SPGPVAEVVS RGDSSVIQTV AGPRGPAGTP GPAGPEGPAG
ADGEPGDPGE DGSQGLVGPP GFPGTPGDSG LKGEKGDRGE GQPGPSGPPG PPGLPAPSSH
NRPTFVDMEG SGFPDLETLR GLPGLPGPPG LPGAPGPAVV GTGLSSSFGP QGPPGQDGAP
GQPGLPGPPG TDGRPAVAGA RGEKGDPGEL GLLGAVGAKG AQGLTGIPGQ PGQGGLAGLP
GPMGPVGQPG PPGPPGPSYH AGFDDMEGSG VGVANGVPGA RGPDGRQGTT GIPGLPGKPG
FPGAPGEKGS EGLQGRDGRP GLDGFPGPNG QKGDRGERGE TGRDGNGQPG PPGPPGPPGQ
IIYQTSSSGG TGLPGQAGFP GPIGPKGDMG DPGQPGYGVK GEKGEPGLII GPDGSPLYLG
ELSGEKGDRG PAGPVGPPGQ YGPSGIKGEF GMPGRPGRPG VNGYKGEKGE PSTGAGFGYP
GVPGPPGPPG PPGPAVPVDR FNGYDASRIY PATKGEKGDH GAQGLPGTPG VASNLDIFTF
KNDLKGERGD SGVKGEKGEP SGGYYDPRFR GQQGPPGPPG NPGLMGPKGD SIMGLPGPQG
PPGSPGIGYD GRPGIPGPPG PPGPPGSPSL PGAYRPNHSI NIPGPPGPAG PPGTPGHTSG
VTVLRSYDTM IATARRQSEG TLIYIVDKTD LYIRVRDGFK QVLLGDYSPF YRDLDNEVAA
VQPPPVVNYP QSQDHSANNG AEHFSQGGSA IHHIKPPPRK PVEIPRPAKP ENRNPDPRYP
PQYDPRYPPQ TDAKYPPQTD GRYSHVQPEN RYPTQPESRF PVTPQRRPIP LPVPQPAGHL
HTSGPGLHLI ALNMPQVGNM RGIRGSDFLC FQQARAVGLK GTFRAFLSSK LQDLYSIVRK
SDRDSLPIIN LRDQVLFNSW ESMFSKTGGR MKENAPIYSF DGRDILRDSA WPEKMVWHGS
SNEGHRQTDN YCETWRAGDR AVTGLASSLQ SGQLLQQLPS SCSSSYIVLC IENSYLSHSK
K
//
