ID A0A6J3JZ07_9HYME Unreviewed; 1159 AA.
AC A0A6J3JZ07;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X7 {ECO:0000313|RefSeq:XP_033345380.1};
GN Name=LOC117231243 {ECO:0000313|RefSeq:XP_033345380.1};
OS Bombus vosnesenskii.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Bombus; Pyrobombus.
OX NCBI_TaxID=207650 {ECO:0000313|Proteomes:UP000504631, ECO:0000313|RefSeq:XP_033345380.1};
RN [1] {ECO:0000313|RefSeq:XP_033345380.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_033345380.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_033345380.1; XM_033489489.1.
DR AlphaFoldDB; A0A6J3JZ07; -.
DR GeneID; 117231243; -.
DR CTD; 104327; -.
DR Proteomes; UP000504631; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; IPR050149; Collagen_superfamily.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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_033345380.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000504631};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1159
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027005425"
FT DOMAIN 45..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 242..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..761
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 121630 MW; A1364E794EA48D07 CRC64;
MRPRLQWLIF VLFCVTRVNA DFFNEKKELE YDLLQASVAL TDDNNLYIDD GLDGFPSFGF
RPGSEVKQPY RLYLPEKLPA EFTLVATFKP TSFRTSYLFA VLNPFETVVQ LGIRISDGPG
TNQNVSLVYT NSDLHSHSEE VAKFTVPKLT KKWSKIVIRV STTDVTLYLN CHEMAKQRVT
RIPLELMFDT ASTLYIAQAG PHIQEKYDGL LQSLKLYSGH PADLVRCTAD FNFNPDEDLG
SGDINNDLID GLEDVDTNVP DIGRDDDEDR SEESNPPPFI TPPPPNPDYK GPKGEKGDKG
DKGESVRGPP GPPGPPGQDE GPPGKKGEPG TCTCNATALM ASFTMPKMIQ GPKGEQGVPG
QEGKQGQMGL TGAAGPPGER GLEGPQGPKG DKGDVGIAGP EGPQGQKGEP GRDGIPGEKG
AQGPPGPPGK GEFSGYDTEG ITMRPGLPGQ KGEAGLPGSP GPKGETGIAG AKGYKGEPGH
KGAKGDHGKE GPRGIQGFKG EPGAPGAPGL PGAPGENGRP AEKGDKGDTG PEGKPGPAGV
PGPPGLPGLS GSGGVNVGEA MLREKGDKGE SGARGYKGDK GTKGEKGDKG DSGPAGIPGV
NGIQGPQGNK GEPGKDGVPG APGVIGAKGE KGERGPPGAT AIASSGDYIT IKGEKGAEGK
RGRRGRPGPP GPVGPPGKTG AMGEIGLPGW AGRPGTPGLP GPVGPVGPKG EKGEPGTPSP
YGVSVGIKGD KGDDGFPGIP GQPGRDGQRG PPGPPGPPGP PSQGNYIPVP GPPGPPGPPG
PPGLSLIGQK GEPGIGRSHI FGERDYYGVR QVPKNIKDFK HNMFFGTLQG PRTSLDELKA
LRELKQLKEL KEHLGAATTA TRGPLESTTK IVPGAVTFQN TEAMTKMSAV SPVGTLAYII
DEQALLVRVN NGWQYIALGS LLPITTPAPP TTSPPPVNPP FEASNLINQI PVKADGTGLR
MAALNEPFTG DMHGVRGADY ACYRQAKRAG LRGTFRAFLS SRVQNVDSIV RLGDRDLPIV
NIKGDVLFNS WKEMFNGNGA YFSQNPRIYS FNGKNILTDF AWPEKVAWHG SHKLGDRAMD
TYCDAWHSSS SDRYGLGSPL TGGRLLEQVR YSCDNKFALL CIEVTSETTR RRRSVEVSED
EDEMSENDYK EYLDSLMEN
//
