ID A0A6J1VEX1_9SAUR Unreviewed; 787 AA.
AC A0A6J1VEX1;
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-like {ECO:0000313|RefSeq:XP_026541822.1};
GN Name=LOC113424374 {ECO:0000313|RefSeq:XP_026541822.1};
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_026541822.1};
RN [1] {ECO:0000313|RefSeq:XP_026541822.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR RefSeq; XP_026541822.1; XM_026686037.1.
DR AlphaFoldDB; A0A6J1VEX1; -.
DR GeneID; 113424374; -.
DR KEGG; nss:113424374; -.
DR Proteomes; UP000504612; Unplaced.
DR GO; GO:0005594; C:collagen type IX trimer; 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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1114; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000504612};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..787
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026800118"
FT DOMAIN 528..571
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 614..783
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 181..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..302
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..336
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 82587 MW; 2238FF024B992DD6 CRC64;
METLKGHQPL GFLCLVLLLG GLTPSSVAQY NWWLFANPKA MTTPAMISQE AKTDVKQFSV
ATVPSSSIPH NTPDTTAKEV PTTEQILDLA TSSSITKEDA FDDNLPVSTF FEGSAMEEGS
EFLMVQEGSK SLTTSDYQSM ITGDTKMTQT TSKVLMTSVQ QSTITGDSMV TPINNISQCV
CPAIPGPPGP KGPKGDQGPP GQKGLTGKIG PTAKPGNPGL PGPQGLPGPV GPPGPPGSTL
PKVIDFTDTR DGEDKRVSFV EGPPGPPGIS GHPGPQGYPG PEGPQGPAGL PGHEGQQGAP
GLPGAPGQPG PPGATGATGI PGPVGSEGPP GVTGPEGHAG IPGQIGSPGL PGFPGPEGPP
GINGSPGQNG PKGEKGDRGE PGLPGKPGQT GEKGAQGPPG PAGPPGLPGD NEYNSKACVQ
GPPGPKGEKG EPGKMECSTC GKDARNDIDS WVAFIYQKGR PGLPGNPGPP GPPGPPGVLY
INRVYPVRPR PHCKQPVNQD PCFDSDIEPP MKDSPDKSQN GYKHPTWTFG SKELMLKSAS
SIPEGSLVYI TEEAEAFFKT PKGWKKILME DSALLFAADD PLVPMENNQV QLDERNVTIP
TIVPTSIPQR IPSLRLVALN FPLTGNMGGI SGVDLQCHRQ AQQANLQGTF RAFLSGNTQS
LISVVKRTDR NLPLVNLKGQ LLAKSWNSLF TMHGNSDFNP MENPIYAFNG LNVMTDPTWT
YKAVWHGFAF QINHSQIRDC ENWRKASKYL RGQASIPLKD IFLLETSWRC SDLLVVLCVE
NSFGVST
//
