ID A0A8C9ETQ6_PAVCR Unreviewed; 1442 AA.
AC A0A8C9ETQ6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSPSTP00000005585.1};
OS Pavo cristatus (Indian peafowl) (Blue peafowl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Pavo.
OX NCBI_TaxID=9049 {ECO:0000313|Ensembl:ENSPSTP00000005585.1, ECO:0000313|Proteomes:UP000694428};
RN [1] {ECO:0000313|Ensembl:ENSPSTP00000005585.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPSTP00000005585.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR Ensembl; ENSPSTT00000005863.1; ENSPSTP00000005585.1; ENSPSTG00000003945.1.
DR Proteomes; UP000694428; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 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; IPR001791; Laminin_G.
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; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000694428};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 132..320
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 181..319
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..336
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..375
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..689
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1074
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1098
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1442 AA; 146929 MW; 19AB7D2A59FD6F9C CRC64;
MGAPEHFEDA RRQPGRTPSA QRGLRSSVPG AGGGLSPPRP RPAPPPPRRA GPSRAARSRA
EPRIAGSGGH HAPGVSGGAG ESGAGDGAEA DSVLCASFSS RRCAPRRLLL LGLFVLLLLP
AASQEPENLS AEVSLLELIG DPPPEEILKI YGPENNPGYV FGPNANTGQV ARYHLPSPFY
RDFSLLFHIQ PTTPRAGVLF AITDSTQSII YVGVKLSDLQ MGKQQIIFYY TEPGSQSSYA
AATFTVPTLL NQWTRFAISV EEDEVILYLD CEEHERVRFE RSPDEMELEE GSGLFVAQAG
GADPDKYQGV IADLRLRGDP RAAEHYCEEE EDDAEASGDF GSGAEDGHRP SGKDKGTPGL
LDAVPVTSPP VVESSGTRSS VGSPQQAERT RVEERLQVST GGTGPKGEKG EKGERGLKGD
SGTSGVLGTG TAKGEKGEKG ELGIKGSAGF GYPGSKGQKG EPGEPGPPGP LSRHTDGMSL
EQVTGPPGPT GPPGKDGAPG RDGEPGDPGE DGKPGEMGPQ GFPGTPGESG QKGEKGDPGV
GPRGPPGPPG PPGPPGPSSK QDGLTFIDME GSGFGGDLET LRGPRGPPGP PGPPGVPGLP
GEPGRFGMNS TDLPGPPGLP GRDGTPGPPG PEGPLGPPGK DGMPGPPGPK GERGDVGDLG
LPGAPGPKGS KGEAGPAGPP GETGLAGLPG PVGPRGQPGP PGPPGPPGPG YEAGFGDMEG
SGLPLATGSP GPRGPSGPQG VPGLPGIKGE VGSLGQPGPP GPKGDAGVPG VDGRPGLEGF
PGPQGPKGNR GSPGEKGERG QDGVGLPGPP GPPGPPGQVI YISSEDRPSV ALPGPGGRPG
HAGFPGPVGP KGDPGSPGIQ GPPGMKGEKG EPGVIISPDG TVVAANVKGQ KGEPGLQGPM
GPSGPQGRAG MKGEIGFPGR PGRPGMNGLK GEKGDPVDIS DVLSLRGPPG PPGPPGPPGP
PGSVVYDSNN GFSDASRPAF PGFHQFPGQK GEKGDVGAPG PPGQFPYDLS RFSASLRGDK
GEAGPKGEKG EPGGSMLYGP SVTGPPGPQG YPGPPGPKGD SIVGPPGPPG PQGPPGIGYE
GRQGPPGPPG PPGPPSFPGP HRQAISIPGP PGPPGPPGPP GASGASLGLR AMPTYQAMLS
AAHELPEGGL IFLADRQELY VRLRGGFRRV LLEEHTLVPS SALDNEVYDK LPSIHYGGAQ
QPVHPLRNHN PPPTARPWRG DEVVANQHRL PQPPLLQQHE LLNSYYIHRW PDPAPVAAHV
HQDFQPALHL VALNTPLSGG MRGIRGADFQ CFQQARQVGL AGTFRAFLSS RLQDLYSIVR
RADRTAVPIV NLRDEVLFSN WEALFTGSEA PLRAGARILS FDGRDILQDS AWPQKSIWHG
SDAKGRRLPE SYCEAWRTDE RGTTGQASSL SSGKLLEQSA SSCQHAFVVL CIENSFMTAA
KK
//
