ID A0A6J3JZ35_9HYME Unreviewed; 1160 AA.
AC A0A6J3JZ35;
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(IX) chain isoform X6 {ECO:0000313|RefSeq:XP_033345379.1};
GN Name=LOC117231243 {ECO:0000313|RefSeq:XP_033345379.1};
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_033345379.1};
RN [1] {ECO:0000313|RefSeq:XP_033345379.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_033345379.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_033345379.1; XM_033489488.1.
DR AlphaFoldDB; A0A6J3JZ35; -.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF958; COLLAGEN ALPHA-1(I) CHAIN; 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_033345379.1};
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..1160
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026972019"
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..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1160
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 765..775
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 121920 MW; 00359BF49ED78C6D 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 ANSMKGRPGT PGLPGPVGPV
GPKGEKGEPG TPSPYGVSVG IKGDKGDDGF PGIPGQPGRD GQRGPPGPPG PPGPPSQGNY
IPVPGPPGPP GPPGPPGLSL IGQKGEPGIG RSHIFGERDY YGVRQGPRTS LDELKALREL
KQLKELKEHL GAATTATRGP LESTTKIVPG AVTFQNTEAM TKMSAVSPVG TLAYIIDEQA
LLVRVNNGWQ YIALGSLLPI TTPAPPTTSP PPVNPPFEAS NLINQIPVKA DGTGWYPRML
RMAALNEPFT GDMHGVRGAD YACYRQAKRA GLRGTFRAFL SSRVQNVDSI VRLGDRDLPI
VNIKGDVLFN SWKEMFNGNG AYFSQNPRIY SFNGKNILTD FAWPEKVAWH GSHKLGDRAM
DTYCDAWHSS SSDRYGLGSP LTGGRLLEQV RYSCDNKFAL LCIEVTSETT RRRRSVEVSE
DEDEMSENDY KEYLDSLMEN
//