ID A0A6J3JZ31_9HYME Unreviewed; 1174 AA.
AC A0A6J3JZ31;
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 X2 {ECO:0000313|RefSeq:XP_033345374.1};
GN Name=LOC117231243 {ECO:0000313|RefSeq:XP_033345374.1};
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_033345374.1};
RN [1] {ECO:0000313|RefSeq:XP_033345374.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_033345374.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_033345374.1; XM_033489483.1.
DR AlphaFoldDB; A0A6J3JZ31; -.
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_033345374.1};
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..1174
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027031602"
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..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1174
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 484..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 123606 MW; EE4C09144D71BDB2 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 GEFSGYDPSW KPRGIYRTEG 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
PVKADGTGWY PRMLRMAALN EPFTGDMHGV RGADYACYRQ AKRAGLRGTF RAFLSSRVQN
VDSIVRLGDR DLPIVNIKGD VLFNSWKEMF NGNGAYFSQN PRIYSFNGKN ILTDFAWPEK
VAWHGSHKLG DRAMDTYCDA WHSSSSDRYG LGSPLTGGRL LEQVRYSCDN KFALLCIEVT
SETTRRRRSV EVSEDEDEMS ENDYKEYLDS LMEN
//
