ID A0A6P3X2M9_DINQU Unreviewed; 1164 AA.
AC A0A6P3X2M9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(V) chain-like isoform X2 {ECO:0000313|RefSeq:XP_014472610.1};
GN Name=LOC106743356 {ECO:0000313|RefSeq:XP_014472610.1};
OS Dinoponera quadriceps (South American ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Dinoponera.
OX NCBI_TaxID=609295 {ECO:0000313|Proteomes:UP000515204, ECO:0000313|RefSeq:XP_014472610.1};
RN [1] {ECO:0000313|RefSeq:XP_014472610.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_014472610.1; XM_014617124.1.
DR AlphaFoldDB; A0A6P3X2M9; -.
DR GeneID; 106743356; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000515204; 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:SF966; COLLAGEN ALPHA-1(XXII) CHAIN-LIKE; 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 Reference proteome {ECO:0000313|Proteomes:UP000515204};
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_5027552353"
FT DOMAIN 35..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 257..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..417
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..563
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..624
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..778
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; 122127 MW; AF856D9BC0F34762 CRC64;
MPPRSSLVIL VALCATCGRA DFFGERKEMV YDLIEATVSS MTTDDNNFYI DDGLDGFPAF
GFRPGSEVKQ PYRLYLPEKL PAEFTLVATF KPTSFRTSYL FAVLNPFETV VQLGIRISDG
PGSNQNVSLV YTNSDEHSHS EEVAKFTVPK LTKKWSKIVI KVSATDVTFY LNCHEMARQR
VTRIPQKLVF DTASTLYIAQ AGPHIQERYD GLLQSLKLYS GHPPDLVKCS TDFNFAEDEE
LSSGDYDGLN LFDGSGDADL NKIGRDADED KSEESNPPPF ITPPPPNPDY KGPKGEKGDK
GDKGESVRGP PGPPGPPGRD EDWLMKIPPQ GPPGQKGDPG TCTCNATALM SSFTMPKMIQ
GPKGEPGVPG QEGKQGQMGL TGAAGPPGER GLQGPSGAKG DKGDIGIPGP EGPQGQKGEP
GRDGIPGEKG AQGPPGPPGK GEFSGYDPSW KPRSIYRTEG ITMRPGLPGQ KGEPGTSGSP
GPKGESGITG SKGIKGEPGH KGAKGDHGKE GPRGTQGFKG EPGAPGAPGL PGAPGENGRP
AEKGDKGDIG PEGKPGPPGP PGSPGTSSSG GINVGDLGFG TKGDKGELGA RGYRGDKGTK
GEKGDKGDAG PAGIPGINGI QGPQGDKGEP GTDGVPGSPG TPGAKGERGE RGPPGATTVA
SSGDYVTIKG EKGAEGKRGR RGRPGPPGPV GPPGKPGIMG EIGLPGWIGR PGNPGLPGSI
GPMGPKGEKG EPGTPSPYGV SVGIKGDKGT DGLPGIPGQT GRDGQRGPPG PPGPPGPPSQ
GKYIPVPGPP GPPGPPGPPG LSLIGQKGEP GIGRSPYGER ETYYGLRQGP RSSLDELKAL
RELKHLKELK EQLGAATAAT RGPLESTTKI VPGAVTFQNT EAMTKMSSVS PVGTLAYIID
EQALLVRVNN GWQYIALGSL LPITTPAPPT TAPPPANPPF EASNLINQIP VKADGTGWYP
RMLRMAALNE PFTGDMHGIR GADYACYRQA RRAGLRGTFR AFLSSRVQNV DSIVRLGDRD
LPIVNIKGDV LFNSWKEMFN GNGAYFSQNP RIYSFNGKNI LTDFAWPEKV AWHGSHKLGD
RAMDTYCDAW HSSSSDRYGL GSPLSGGRLL EQVRYSCDNK FALLCIEVTS EAVRRRRSAD
DRLEDDVEMT ENDYVEYLEE LMQY
//
