ID A0A8C9ETK0_PAVCR Unreviewed; 1422 AA.
AC A0A8C9ETK0;
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:ENSPSTP00000005648.1};
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:ENSPSTP00000005648.1, ECO:0000313|Proteomes:UP000694428};
RN [1] {ECO:0000313|Ensembl:ENSPSTP00000005648.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPSTP00000005648.1}
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; ENSPSTT00000005929.1; ENSPSTP00000005648.1; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1019; COLLAGEN ALPHA-5(IV) CHAIN ISOFORM X1; 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..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1107
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 344..355
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..669
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1037
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1054
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 144972 MW; 6E23B435CB17954E 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 EDDAEGTPGL 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
//
