ID A0A1S3R0M3_SALSA Unreviewed; 1380 AA.
AC A0A1S3R0M3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X2 {ECO:0000313|RefSeq:XP_014045910.1};
GN Name=LOC106599284 {ECO:0000313|RefSeq:XP_014045910.1};
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_014045910.1};
RN [1] {ECO:0000313|RefSeq:XP_014045910.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014045910.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014045910.1; XM_014190435.1.
DR GeneID; 106599284; -.
DR OrthoDB; 5363002at2759; -.
DR Proteomes; UP000087266; Chromosome ssa03.
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:SF1099; COLLAGEN ALPHA-1(XV) CHAIN ISOFORM X1; 1.
DR Pfam; PF01391; Collagen; 4.
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_014045910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010230194"
FT DOMAIN 112..303
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 72..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1099
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 142150 MW; 17B59412D5C75704 CRC64;
MAVLRLCSLL LLLMAPVHGQ WWSVLWGKAQ EMTTQPPTTE VLTTTKVFWT MEGTEVGQVG
TQTEVYTTAP VQSTPLQSTQ EPAGAGTTEI KPNAKKRPLK MWKSREHGST GHLDLTELIG
VPLPPSVSYI TGYEGFRPAY NFGPGANIGR LTKTFMPDPF FRDFAIIVTI RPSSNQGGVL
FAITDAQQKV VQLGLALTAV EDETQRIQLY YTEGGQGSSH SQQVVSFKVP DMTKKWTIFT
LSVQDQEVCL YMDCDDFQAE TFHRSSRQLS FEPSSGIFVG NAGGTGLERF MGSIQQLVIK
SDPRAAEEQC EEDDPYASGD GSGAETMDDR ETEGLMKNTK RRKETARPED MLSGPVRAPP
TESPEVELDE YSGHLTPTEE ANQEMLLRGP HQTEEPEMSG DGGPLSHRQK GERGEPGPMG
PAGPRGPPGP PTPSEGRRSG HGQPGPRGPR GSSGPTGAPG VPGKDGQQGS KGDDGDPGQR
GPQGFPGLAG EVGVKGDKGD PGAGLPGPPG PPGPPGPLRS HSVPYGEDAL GSGFGDLDNT
ELIRGPPGPP GQPGPPGPTS PFNASEGLFT GQPGPPGRYG LVGKPGPPVN EDWFSGSGLG
SGFGSEFGSG LFGSGLGSGE GQPGLDGEVG PTGPKGLKGE QGLVGPKGES GDLGLAGATG
PRGPEGKRGD TGPRGLPGPP GPPGAGLFVE DMEGSGKNDM LLGVGLKGPQ GPPGLPGPAG
PKGEDGKDGA PGLSVKGEPG APGPEGLQGL AGLPGARGLK GDKGDPGPKG ECGPDGHTVP
GSPGPPGSPG PIINLQDLLL NDTEGMFNQI RGAPGPMGPE GEPGRAGFPG PRGPKGDIGL
PGLHGPPGMK GAKGESGVTI AADGTVLTGV RGPQGPKGIK GERGFPGVAG IMGPIGPTGQ
KGEYGFPGRP GRPGMAGKKG DKGDAIGQPG LPGPPGPPGP VIGLNGTVFP VRPRPFCKTP
VNGSRGSSQG SRRGNRGAKG EKREVGLPGT PGEPDDVLPE GFVGEKGDVG YEGMKGEKGD
AGLPGPPGLP GRSGLVGPKG ESIVGAPGHP GAPGEPGVPG IGRPGTRGPP GPAGPPGPPP
VYASAVSIPG PPGPPGPPGI TGNENLVTTY RNTITLMRES HRAAEGSMAY VSDKGELYVR
ARDGWRKVQL GELIPVPAET PSSALSQALS RPGDRSRPHR QELVGTSYMP NYNVLPHTVH
SVPGLHLVAL NAPFSGDMGG IRGADFQCYQ QARAMGLTST YRAFMSSHLQ DLATIVKKGD
RYSMPVINLK GEVLYGSWMN IFSGNGGVLE PSIPIYSFDG RNVMTDPTWP QKLVWHGSST
VGIRMTTNYC EAWRAGDMAV TGQASLLQTG RLLGQHTRSC SNRFVVLCIE NSYIDHRMSN
//
