ID A0A6J3JYK7_9HYME Unreviewed; 1149 AA.
AC A0A6J3JYK7;
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 X8 {ECO:0000313|RefSeq:XP_033345381.1};
GN Name=LOC117231243 {ECO:0000313|RefSeq:XP_033345381.1};
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_033345381.1};
RN [1] {ECO:0000313|RefSeq:XP_033345381.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_033345381.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_033345381.1; XM_033489490.1.
DR AlphaFoldDB; A0A6J3JYK7; -.
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:SF1109; COLLAGEN ALPHA-4(IV) CHAIN-LIKE; 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_033345381.1};
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..1149
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027050163"
FT DOMAIN 45..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 233..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..746
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1136
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 120966 MW; FE5C292CEA170209 CRC64;
MRPRLQWLIF VLFCVTRVNA DFFNEKKELE YDLLQASVAL TDDNNLYIDD GLDGFPSFGF
RPGSEVKQPY RLYLPEKLPA EFTLVATFKP TSFRTSYLFA VLNPFETVVQ LGIRISDGPG
TNQNVSLVYT NSDLHSHSEE VAKFTVPKLT KKWSKIVIRV STTDVTLYLN CHEMAKQRVT
RIPLELMFDT ASTLYIAQAG PHIQEKYDGL LQSLKLYSGH PADLVRCTAD FNIGRDDDED
RSEESNPPPF ITPPPPNPDY KGPKGEKGDK GDKGESVRGP PGPPGPPGQD EGPPGKKGEP
GTCTCNATAL MASFTMPKMI QGPKGEQGVP GQEGKQGQMG LTGAAGPPGE RGLEGPQGPK
GDKGDVGIAG PEGPQGQKGE PGRDGIPGEK GAQGPPGPPG KGEFSGYDPS WKPRGIYRTE
GITMRPGLPG QKGEAGLPGS PGPKGETGIA GAKGYKGEPG HKGAKGDHGK EGPRGIQGFK
GEPGAPGAPG LPGAPGENGR PAEKGDKGDT GPEGKPGPAG VPGPPGLPGL SGSGGVNVGE
AMLREKGDKG ESGARGYKGD KGTKGEKGDK GDSGPAGIPG VNGIQGPQGN KGEPGKDGVP
GAPGVIGAKG EKGERGPPGA TAIASSGDYI TIKGEKGAEG KRGRRGRPGP PGPVGPPGKT
GAMGEIGLPG WANSMKGRPG TPGLPGPVGP VGPKGEKGEP GTPSPYGVSV GIKGDKGDDG
FPGIPGQPGR DGQRGPPGPP GPPGPPSQGN YIPVPGPPGP PGPPGPPGLS LIGQKGEPGI
GRSHIFGERD YYGVRQVPKN IKDFKHNMFF GTLQGPRTSL DELKALRELK QLKELKEHLG
AATTATRGPL ESTTKIVPGA VTFQNTEAMT KMSAVSPVGT LAYIIDEQAL LVRVNNGWQY
IALGSLLPIT TPAPPTTSPP PVNPPFEASN LINQIPVKAD GTGWYPRMLR MAALNEPFTG
DMHGVRGADY ACYRQAKRAG LRGTFRAFLS SRVQNVDSIV RLGDRDLPIV NIKGDVLFNS
WKEMFNGNGA YFSQNPRIYS FNGKNILTDF AWPEKVAWHG SHKLGDRAMD TYCDAWHSSS
SDRYGLGSPL TGGRLLEQVR YSCDNKFALL CIEVTSETTR RRRSVEVSED EDEMSENDYK
EYLDSLMEN
//
