ID A0A6P9C112_PANGU Unreviewed; 1548 AA.
AC A0A6P9C112;
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 isoform X4 {ECO:0000313|RefSeq:XP_034276144.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_034276144.1};
OS Pantherophis guttatus (Corn snake) (Elaphe guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Colubrinae; Pantherophis.
OX NCBI_TaxID=94885 {ECO:0000313|Proteomes:UP001652622, ECO:0000313|RefSeq:XP_034276144.1};
RN [1] {ECO:0000313|RefSeq:XP_034276144.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_034276144.1};
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_034276144.1; XM_034420253.2.
DR GeneID; 117667073; -.
DR CTD; 80781; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP001652622; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR010363; DUF959_COL18_N.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR37456:SF5; COLLAGEN TYPE XIII ALPHA 1 CHAIN; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 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_034276144.1};
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:UP001652622};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1548
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027892735"
FT DOMAIN 223..411
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 38..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..102
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..623
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..725
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..756
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..883
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1046
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1134
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1548 AA; 160632 MW; C295D10AD35007FF CRC64;
MARVIVSAWL LLMLLCCLAN AQGWRNWFWS GSEETTLSPT KAAEAEDETS QDHSTPAATA
RPNAPFESTT DPEPRGKAGT IFTLKQPDFT PTVPVPAATS PSQEESRERN ITGVGVEILN
VAEGIQNLVQ LLDEKTTDRT ERTEVPATTE TSASPAPVTE PGSIQNVTSN LTGDIQTSLK
TKKPEGATKL ARLWNKDLAL LWNKTRVFPK KPGKPRQENF SREVGLLELI GDPPPDQITK
IYGPDKSPAY VFSPDANAGQ VARYHLPSPF YRDFSLLFYI QSTSDNAGVL FALTDASQSI
IYVGVKLSEV KDGKQQIIFY YTEPGSQNSN VAATFTVPSL VNLWTRFALS VRDYNVVLYM
DCEEFKMVHL ERSSGKIELE EGAGLFVGQA GGADPDKYQG IIVELKIKDN PWAAGYQCVE
EDDDCDTCGG SGSGLDIKQP PSEKESVIPL LSKLPVPPPV TSPAIAKKPV QLEETEYTER
PTYVPASGTK GEKGDPGEKG DRGPKGDPGT GVLSTNGDKG EKGEKGELGV KGSAGFGYPG
SKGQKGEPGT TGLPGPIGPP GPPGTIMRHS DGSTVEGPGA MGPPGLPGKD GQPGKDGEPG
DPGEDGKPGD VGPQGFPGTP GEPGLKGEKG EPSVGARGPP GPPGPPGKPG LSSKVDKLTF
IDMEGSGFGS ELESLRGPRG PPGPPGPPGV PGLPGQPGRF GTNGTDFPGL PGLPGVPGRN
GNSGIPGPPG PLGPPGKDGI PGQPGEKGAP GEPGEMGFPG APGPEGNQGV PGFPGTPGEP
GLAGLPGPMG PRGLPGPPGP GIAAEFVDME GSGFPLVSGG PGTRGPEGPP GLPGLPGLPG
PPGPKGDEGI IGLPGLPGEK GYPGLPGLDG RPGLEGFPGP QGQKGEEGSP GSKGEKGQDG
IGLPGPPGPP GQAVYLSSED KTVPVLPGPE GPKGPKGDSG TPGLQGYPGL KGEKGEPGVV
TRPDGTILAA EAKGEKGEPG PSGPMGPGGP PGRYGRKGEL GFPGRPGRPG MNGLKGEKGD
PADLSGALGL RGPPGPPGPP GPPGSPVPVY ENNAFSDLGP PGPPGLPGYH GQKGEKGEQG
LPGPPGQFPY DLSRFSSTFR GERGDKGDPG MKGEKGESGG GSNAAGLPGP QGYPGLPGPK
GESIRGLPGP PGPQGPPGAG FEGHPGPQGP PGPPGPPGPP SFPGPHRQHI SIPGPPGPPG
PPGPPGTSDP PSLGVRILAT YQNLMSRAHE VPEGQLLFIR EREELYIRVH NGFRKILMEE
KISIPGSGLD NEVYERSSSI HYSHGGTASS GSHRPFQPHL PVHARPEYSA YSTAKPWRGD
ESIIDPHHLP EQPAVHPPRQ GAQQESLDHF FPNNRQTETA PLAVHTHHDF QPALHLIALN
SPQSGSMRGI RGADFQCFQQ ARQVGLPGTF RAFLSSRLQD LYSIVRRADR STVPIVNLRD
EVLFNNWENL FSGSEAPFRT GVRILSFDGR DVLRDSAWPQ KYVWHGSDSK GRRLTESYCE
TWRTDDTVVT GQASSLASSK LLEQKSNSCR NAFIVLCIEN SFMTSSKK
//
