ID A0A8C6VAE7_NAJNA Unreviewed; 1522 AA.
AC A0A8C6VAE7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSNNAP00000002695.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSNNAP00000002695.1};
OS Naja naja (Indian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=35670 {ECO:0000313|Ensembl:ENSNNAP00000002695.1, ECO:0000313|Proteomes:UP000694559};
RN [1] {ECO:0000313|Ensembl:ENSNNAP00000002695.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSNNAP00000002695.1}
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; ENSNNAT00000002834.1; ENSNNAP00000002695.1; ENSNNAG00000001829.1.
DR GeneTree; ENSGT00940000158212; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000694559; 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; IPR010363; DUF959_COL18_N.
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; 4.
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 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:UP000694559};
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..1522
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034657926"
FT DOMAIN 225..413
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 38..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..104
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..616
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..718
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..773
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..831
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..870
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..964
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1108
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1522 AA; 157681 MW; 24092CCED501EF2F CRC64;
MARVIVSAWL LLVLLCCLAS AQGWRNWFWS GAEKTTLSPT RAAKAEDETS QDPSTSAAAT
ASPDAPFEST TDPEPRGKAG TIFTLKQPDF APTVPVPAAA TSPSQEEGRG RNITGVGVEI
LSVAEGIQNV VQLLDEKTAD RMEGTEVPDT TEANASPAPG MEPGSIQNVT ANLTSGIQTS
LKTKKPEGPT KLARLWNKDL ALLLNKTRAF PKKPGKPRQE NFSREVGLLE LIGDPPPDQI
TKIYGPDKSP AYVFRPDANA GQVARYHLPS PFYRDFSLLF YIQSTSDNAG VLFALTDASQ
SIIYVGVKLS EVKDGKQQII FYYTEPGSQN SNVAATFTVP SLVNLWTRFA LSVRDYSVVL
YMECEEFKTV HLERSSGKIE LEEGAGLFVG QAGGADPDKY QGIIVELKIK DNPWAAGYQC
VEEDDDCDTC GGSGSGLDIK QPSSEKESVI PLLSNLPLPT PVTSPAIAKK PVQLEETEYI
ERPTYVPASG TKGEKGDPGE KGDRGPKGDP GTGVLSTNGD KGEKGSAGFG YPGSKGQKGE
PGTPGLPGQI GPPGPPGTIM RHSDGSTVEH PGAMGPPGLP GKEGQPGKDG EPGDPGEDGK
PGDVGPQGFP GTPGEPGLKG EKGEPGVGAR GPPGPPGPAG KPGLSSKLDK LTFIDMEGSG
FGSELESLRG PKGPPGPPGP PGVPGLPGQP GRFGTNGTDL PGLPGLPGVP GRNGNSGIPG
PPGPLGPRGK DGIPGQPGEK GAPGEPGEMG FPGPQGSQGK PGLPGEPGLA GLPGPMGPRG
LPGPPGPGIA AEFVDMEGSG FPFVSGGPGT RGPEGPPGLP GLPGLPGPPG PKGDEGIIGL
PGLPGEKGYP GLPGLDGRPG LEGFPGPQGQ KGEEGSKGEK GQDGIGLPGP PGPPGQAVYL
SSEDGLKGPK GDSGTPGLQG YPGLKGEKGE PGVTTRSGGT ILAAEAKGER GEPGPSGPMG
PAGPPGRYGR KGELGFPGRP GRPGMNGLKG EKGDPADLSG ALGLRGPPGP PGPPGPPGSP
VPVYENNAFS DLGPPGPPGL PGYHGQKGEK GEQGLPGPPG QFPYDLSRFS STFRGETGDK
GDPGMKGEKG ESGGGSSAAG LPGPQGYPGL PGPKGESIRG LPGPPGPQGP PGAGFEGRPG
PQGPPGPPGP PGPPSFPGPH RQHISIPGPP GPPGPPGPPG ISDLPSLGVR ILATYQNLMS
RAHEVPEGQL LFIQDREELY IRVHNGFRRI LLEEKISIPG TGLDNEVYER SSSIHYSHGG
TASSGSHRQF QPHLPVHARP EYSAYSTAKP WRGDESMVDP HHLPEQPAVH PPRQGAQQES
LDHFFPNNRQ TETAPLAVHT HHDFQPALHL IALNSPQSGS MRGIRGADFQ CFQQARQVGL
SGTFRAFLSS RLQDLYSIVR RADRSTVPIV NLRDEVLFNN WENLFSGSEA PFRTGVRILS
FDGRDVLRDS AWPQKYMWHG SDSKGRRLTE SYCETWRTDD TVVTGQASSL ASGKLLEQKS
NSCRNAFIVL CIENSFMTSS KK
//
