ID A0A6I9WIY2_9HYME Unreviewed; 1161 AA.
AC A0A6I9WIY2;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XXII) chain isoform X3 {ECO:0000313|RefSeq:XP_011642988.1};
GN Name=LOC105430905 {ECO:0000313|RefSeq:XP_011642988.1};
OS Pogonomyrmex barbatus (red harvester ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Pogonomyrmex.
OX NCBI_TaxID=144034 {ECO:0000313|Proteomes:UP000504615, ECO:0000313|RefSeq:XP_011642988.1};
RN [1] {ECO:0000313|RefSeq:XP_011642988.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_011642988.1; XM_011644686.2.
DR AlphaFoldDB; A0A6I9WIY2; -.
DR GeneID; 105430905; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000504615; 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_011642988.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000504615};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1161
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026737923"
FT DOMAIN 34..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 262..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..413
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..577
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..620
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..795
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1161 AA; 122036 MW; B429920488A7969D CRC64;
MLPRSLLVIF AALCATYGRA DFFSGKEVVY DLMEASVSSM TDDNNLYMDD GVDGFPAFGF
RPGSEVKQPY RLYLPEKLPA EFTLVATFKP TSFRTSYLFA VLNPFETVVQ LGIRISDGPG
SNQNVSLIYT NSDEHSHSEE VAKFTVPKLT KKWSKIVIKV SINDVTFYLN CHEMARQRVT
RIPQELVFDT ASTLYIAQAG PHIQERYDGL LQSLKLYSGH PPDLVKCTSD FDFSADEELS
SGDYDLNLYD GSGDAEFNKI SRDADEDKSE ESNPPPFITP PPPNPDYKGP KGEKGDKGEK
GESVRGPPGP PGPPGRDEDW LMKIPQGPPG QKGDTGSCTC NATALMSSFT MPKMIQGPKG
EPGVPGQEGK QGLMGLTGAA GPPGERGLQG PSGAKGDKGD IGIPGPEGPQ GQKGEPGRDG
IPGEKGAQGP PGPPGKGEFS GYDPSWKPRN IYRPEGITMR PGLPGQKGEP GTSGSPGPKG
ESGIPGSKGI KGEPGHKGAK GDHGKDGPRG IQGFKGEPGA PGAPGLPGAP GENGRPAEKG
DKGDTGPEGK PGPPGPPGPS GIGGPGGINV GDLGFGIRGD KGDSGARGYK GDKGTKGEKG
DKGDSGPAGI PGINGIQGPQ GDKGEPGKDG VSGLPGIPGT KGERGERGPP GATTIANSGD
YITIKGEKGA EGKRGRRGRP GPPGPVGPPG KPGITGEIGL PGWMGRPGTP GIPGSIGPMG
PKGEKGEPGA PSPYGVSLGI KGDKGDDGFP GIPGQPGRDG QRGPPGPPGP PGAPSQGKYI
PVPGPPGPPG PPGPPGLSLI GQKGEPGIGR SHVFGERDYY GPRQGARSSL DELKALRELK
QLKELKEQLG VVTAATRGPL ESTTKIVPGA VTFQNTEAMT KMSSVSPVGT LAYIIDEQAL
LVRVNNGWQY IALGSLLPIT TPAPPTTSPP PANPPFEASN LINQIPVKAD GTGQWYPRML
RMAALNEPFT GDMHGIRGAD YACYRQARRA GLRGTFRAFL SSRVQNVDSI VRLGDRDLPI
VNIKGDVLFN SWKEMFNGNG AYFSQNPRIY SFNGKNILTD FAWPEKVAWH GSHKLGDRAM
DTYCDAWHSS SSDRYGLGSP LTGGRLLEQV RYSCDNKFAL LCIEVTSELG RRRRSAGNRP
DDDIEMTEND YMEYLEELMQ Y
//
