ID A0A6I9WTD3_9HYME Unreviewed; 1164 AA.
AC A0A6I9WTD3;
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 X2 {ECO:0000313|RefSeq:XP_011642987.1};
GN Name=LOC105430905 {ECO:0000313|RefSeq:XP_011642987.1};
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_011642987.1};
RN [1] {ECO:0000313|RefSeq:XP_011642987.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_011642987.1; XM_011644685.2.
DR AlphaFoldDB; A0A6I9WTD3; -.
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 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; 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_011642987.1};
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..1164
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026707268"
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..820
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 709..725
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..799
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 122364 MW; D448D7B561417F16 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 PGWMNTIKGR PGTPGIPGSI
GPMGPKGEKG EPGAPSPYGV SLGIKGDKGD DGFPGIPGQP GRDGQRGPPG PPGPPGAPSQ
GKYIPVPGPP GPPGPPGPPG LSLIGQKGEP GIGRSHVFGE RDYYGPRQGA RSSLDELKAL
RELKQLKELK EQLGVVTAAT RGPLESTTKI VPGAVTFQNT EAMTKMSSVS PVGTLAYIID
EQALLVRVNN GWQYIALGSL LPITTPAPPT TSPPPANPPF EASNLINQIP VKADGTGWYP
RMLRMAALNE PFTGDMHGIR GADYACYRQA RRAGLRGTFR AFLSSRVQNV DSIVRLGDRD
LPIVNIKGDV LFNSWKEMFN GNGAYFSQNP RIYSFNGKNI LTDFAWPEKV AWHGSHKLGD
RAMDTYCDAW HSSSSDRYGL GSPLTGGRLL EQVRYSCDNK FALLCIEVTS ELGRRRRSAG
NRPDDDIEMT ENDYMEYLEE LMQY
//
