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Database: UniProt
Entry: A0A6J3JX02_9HYME
LinkDB: A0A6J3JX02_9HYME
Original site: A0A6J3JX02_9HYME 
ID   A0A6J3JX02_9HYME        Unreviewed;      1168 AA.
AC   A0A6J3JX02;
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 X4 {ECO:0000313|RefSeq:XP_033345377.1};
GN   Name=LOC117231243 {ECO:0000313|RefSeq:XP_033345377.1};
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_033345377.1};
RN   [1] {ECO:0000313|RefSeq:XP_033345377.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_033345377.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_033345377.1; XM_033489486.1.
DR   AlphaFoldDB; A0A6J3JX02; -.
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   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; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 3.
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_033345377.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000504631};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1168
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5027003794"
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..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1140..1168
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        755..765
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..786
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1146..1155
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1168 AA;  122825 MW;  70CCA417623EDF87 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 ANSMKGRPGT PGLPGPVGPV GPKGEKGEPG
     TPSPYGVSVG IKGDKGDDGF PGIPGQPGRD GQRGPPGPPG PPGPPSQGNY IPVPGPPGPP
     GPPGPPGLSL IGQKGEPGIG RSHIFGERDY YGVRQVPKNI KDFKHNMFFG TLQGPRTSLD
     ELKALRELKQ LKELKEHLGA ATTATRGPLE STTKIVPGAV TFQNTEAMTK MSAVSPVGTL
     AYIIDEQALL VRVNNGWQYI ALGSLLPITT PAPPTTSPPP VNPPFEASNL INQIPVKADG
     TGWYPRMLRM AALNEPFTGD MHGVRGADYA CYRQAKRAGL RGTFRAFLSS RVQNVDSIVR
     LGDRDLPIVN IKGDVLFNSW KEMFNGNGAY FSQNPRIYSF NGKNILTDFA WPEKVAWHGS
     HKLGDRAMDT YCDAWHSSSS DRYGLGSPLT GGRLLEQVRY SCDNKFALLC IEVTSETTRR
     RRSVEVSEDE DEMSENDYKE YLDSLMEN
//
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