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Database: UniProt
Entry: A0A6J3JZ35_9HYME
LinkDB: A0A6J3JZ35_9HYME
Original site: A0A6J3JZ35_9HYME 
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.
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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
//
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