ID A0A6P6GZF9_PUMCO Unreviewed; 1334 AA.
AC A0A6P6GZF9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_025768812.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_025768812.1};
OS Puma concolor (Mountain lion) (Felis concolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Puma.
OX NCBI_TaxID=9696 {ECO:0000313|Proteomes:UP000515131, ECO:0000313|RefSeq:XP_025768812.1};
RN [1] {ECO:0000313|RefSeq:XP_025768812.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025768812.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_025768812.1; XM_025913027.1.
DR GeneID; 112849411; -.
DR KEGG; pcoo:112849411; -.
DR CTD; 80781; -.
DR Proteomes; UP000515131; 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:0032836; P:glomerular basement membrane development; 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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 5.
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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_025768812.1};
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:UP000515131};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 61..249
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 252..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..528
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..548
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..583
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..848
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1013
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1334 AA; 135068 MW; 6875B64672CCA85D CRC64;
MGVVEVEWGP SMGRRWGAAP GTLSGLPHRI LAPLVGAVPV ASPLGLLTGV SLLFAESLGT
EVGLLQLLGE PPPQQVAQVD DPDVGPAFVF GPDANSGQVA RYHFPSPFFR DFSLLFHVRP
ATEGAGVLFA ITDAAQAVVS VGVKLSAVRD GQQHIQLLYT EPGATRTRTA ASFRLPAFTG
QWTRFALSVD GATVALFVDC ELFQRVPLVR SPRALELEPG AGLFVAQAGG ADPSKFQGRI
AELRVRGDPR VSPLHCLEED DEDSGGVSGD FGSGLEENRE LLREQSGLSP KPSLPEAPPV
TSPPLAEGRN VEDSRTEEIE EETTMSSLGA WTLPGSDTVT AWSVRSPGGG PEEPVPSPLR
PQGPAGSAVQ SPDAQPVPGP QGPPGPPGPP GKDGAPGKDG EPGDPGEDGK PGDPGPQGFP
GTPGDMGPKG EKGDPGVGPR GPPGPQGPPG PPGPSFRHDR LTFIDMEGSG FGGDLESLRG
PRGFPGPPGP PGVPGLPGEP GRFGMNSSDV PGPAGLPGVP GRDGAPGLPG APGPPGPPGR
DGGPGKTGQK GSPGEAGAPG PKGSKGDPGP TGAPGETGLA GAPGPAGPPG PPGPPGPPGP
GLAAGFEDMD GSGGPFWSTA HGAGGPQGPP GLPGVKGDPG IAGPPGAKGE VGADGPPGFP
GLPGREGTAG AQGPKGEKGT QGEKGDPGRD GVGQPGLPGP PGPPGPVVYV SEQDRAVAGM
PGPEGRPGYA GFPGPAGPKG DLGSKGQRGP PGPKGEKGEP GPVFSPDGGT LGPAQKGAKG
EPGFRGPPGP YGRPGHKGEI GFPGRPGRPG MNGLKGEKGE PGHASVGFGV RGPPGPPGPP
GPPGPPGTPV YDSNAFMESG RPGPPGLPGY QGPPGPKGDK GEVGPPGPPG QFPLDLLHLE
AEMKGEKGDR GDPGQKGERG EPGGGGFFGS SVPGPPGPPG YPGIPGPKGE SIRGQPGPPG
PQGPPGIGHE GRQGPPGPPG PPGPPGPPSF PGPYRQTISV PGPPGPPGPP GPPGTMGTSS
GVRIWATYQT MLDKVPEVPE GWLIFVAETE ELYVRVRNGF RKVLLEARTP LPRGTDNEVA
ALQPPLVQLH EGNPYPRREL THSTARPWRA DDILAGPPHL PDPRPYPGAP HHGPYLRVQP
ARPTGGPART HTHQDFQPVL HLVALNSPQP GGMRGIRGAD FQCFQQARAV GLAGTFRAFL
SSRLQDLYSI VRRADRTGVP IVNLRDEVLF PSWEALFSGS EGQLKPGARV FSFDGRDVLQ
HPAWPQKSVW HGSDPSGRRL TDSYCETWRT EDAAAAGQAS SLLAGRLLAQ KAASCRNAFI
VLCIENSFMT SSSK
//
