ID A0A6J1VMD0_9SAUR Unreviewed; 1545 AA.
AC A0A6J1VMD0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X2 {ECO:0000313|RefSeq:XP_026541149.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_026541149.1};
OS Notechis scutatus (mainland tiger snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Hydrophiinae; Notechis.
OX NCBI_TaxID=8663 {ECO:0000313|Proteomes:UP000504612, ECO:0000313|RefSeq:XP_026541149.1};
RN [1] {ECO:0000313|RefSeq:XP_026541149.1}
RP IDENTIFICATION.
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_026541149.1; XM_026685364.1.
DR GeneID; 113423810; -.
DR CTD; 80781; -.
DR Proteomes; UP000504612; 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:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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 ECO:0000313|RefSeq:XP_026541149.1};
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:UP000504612};
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..1545
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026666596"
FT DOMAIN 224..412
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 38..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..564
FT /note="Pro 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 824..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..880
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1131
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1180
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 160207 MW; 7745995F15D4013C CRC64;
MARVIVSAWL LLVLLCCLAN AQGWRNWFWS NSKETTLSPT RAAEAEDETS QDPSTPAATA
SQDAPFESTT DPEPRGKAGT IFTLKQPDFT PTIPVPAAAT SPSQEEGRGR NITGVGVEIL
SVAEGIQNLV QLLDEKTTNR TEGTEVPTTT KARASPNPVM EPGSIQNITA NLTGDIQTSL
KTKKPEGATK LARLWNKDLA LLWNKTRAFP KKPGKPRQEN FSREVGLLEL IGDPPPDQIT
KIYGPDKSPA YVFRPDANAG QVARYHLPSP FYRDFSLLFY IQPTSDNAGV LFALTDASQS
IIYVGVKLSE VKDGKQQIIF YYTEPGSQNS NVAATFSVPS LVNLWTRFAL SVRDYNVVLY
MECEEFKTVH LERSSGKIEL EEGAGLFVGQ AGGADPDKYQ GIIVELKIKD NPWAAGYQCV
EEDDDCDTCG GSGSGLDIKQ PSSEKESVIP LLSNLPLPTP VTSPAVAKKT VQLEETEYIE
RPTYVPASGT KGEKGDPGEK GGRGPKGDPG TGVLSTSGDK GEKGEKGELG VKGSAGFGYP
GSKGQKGEPG TPGLPGPIGP PGPPGTIMRH DGSTVEHPGA MGPPGLPGKE GQPGKDGEPG
DPGEDGKPGD VGPQGFPGTP GEPGLKGEKG EPSVGARGPP GPPGPPGKPG LSSKLDKLTF
IDMEGSGFGS ELESLRGPKG PPGPPGPPGV PGLPGQPGRF GTNGTDFPGL PGLPGVPGRN
GNSGIPGPPG PLGPPGKDGI PGQPGEKGAP GEPGEMGFPG QKGSQGVPGL PGSPGEPGLA
GLPGPMGPRG FPGPPGPGIA AEFVDMEGSG FPFVSGGPGT RGPEGPPGLP GLPGLPGPPG
PKGDEGIIGL PGLPGEKGYP GLPGLDGRPG LEGFPGPQGQ KGEEGGPGSK GEKGQDGIGL
PGPPGPPGPA VYLSSEDKIA PVLPGPEGPK GPKGDSGTPG LQGYPGLKGE KGEPGVITTP
DGTILAAEAK GEKGEPGPSG PMGPAGSPGR YGRKGELGFP GRPGRPGMNG LKGEKGDPAD
LSGALGLRGP PGPPGPPGPP GSPVPVYENN AFSDLGPPGP PGLPGYHGQK GEKGEQGIPG
PPGQFPYDLS RFSSTFRGET GEKGDPGMKG EKGESGVGSS AAGLPGPQGY PGLPGPKGES
IRGLPGPPGP QGPPGAGFEG HPGPQGPPGP PGPPGPPSFP GPHRQHISIP GPPGPPGPPG
PPGISDPPSL GVRILATYQN LMSRAHEVPE GQLLFIQDRE ELYIRVHNGF RRILLEERIS
IPGSGLDNEV YERSSSIHYS HGGTASSGSH RPFQPHLPVH ARPEYNAYST AKPWRGDESV
VDPHHLPEQP AVHPPRQGAQ QESLDHFFPN NRQTETAPLA VHTHHDFQPA LHLIALNTPQ
SGSMRGIRGA DFQCFQQARQ VGLSGTFRAF LSSRLQDLYS IVRRADRSTV PIVNLRDEVL
FNNWENLFSG TEAPFRTGVR ILSFDGRDVL RDSAWPQKYM WHGSDSKGRR LTESYCETWR
TDDTVVTGQA SSLASGKLLE QKSNSCRNAF IVLCIENSFM TSSKK
//
