ID A0A6P9BXT4_PANGU Unreviewed; 1847 AA.
AC A0A6P9BXT4;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_034276142.1};
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_034276142.1};
RN [1] {ECO:0000313|RefSeq:XP_034276142.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_034276142.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: May regulate extracellular matrix-dependent motility and
CC morphogenesis of endothelial and non-endothelial cells; the function
CC requires homotrimerization and implicates MAPK signaling.
CC {ECO:0000256|ARBA:ARBA00053766}.
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000256|ARBA:ARBA00054383}.
CC -!- SUBUNIT: Forms homotrimers. Recombinant non-collagenous domain 1 has
CC stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower
CC affinity to FBLN1 and FBLN2 than endostatin.
CC {ECO:0000256|ARBA:ARBA00065165}.
CC -!- SUBUNIT: Monomeric. Interacts with KDR/VEGFR2. Interacts with the
CC ITGA5:ITGB1 complex. Interacts with NID1, HSPG2, laminin-1:NID1
CC complex, FBLN1 and FBLN2. {ECO:0000256|ARBA:ARBA00064471}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_034276142.1; XM_034420251.2.
DR GeneID; 117667073; -.
DR CTD; 80781; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP001652622; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
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 Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_034276142.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1847
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028160757"
FT DOMAIN 403..521
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
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 279..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..1513
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 282..294
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..922
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1024
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1055
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1182
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1433
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 418..464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 455..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1847 AA; 192947 MW; 034907C6124A7779 CRC64;
MARVIVSAWL LLMLLCCLAN AQGWRNWFWS GSEETTLSPT KAAEAEDETS QDHSTPAATA
RPNAPFESTT DPEPRGKAGT IFTLKQPDFT PTVPVPAATS PSQEESRERN ITGVGVEILN
VAEGIQNLVQ LLDEKTTDRT ERTEVPATTE TSASPAPVTE PGSIQNVTSN LTGDIQTSLK
TKKPEGATKL ARLWNKDLAL LWNKTRVFPK KPGKPRQGSA SFSFSPDGHF SGTMLVFQES
PEAGQEVAFT PPAIRATWGA FSKKQGILST AKALKLQESQ ANSSSSSGSN SNSSLHAGMP
SKVVGTLDSW VLPYVTNPSQ PVSKDSGAHL SFKSHPFFKH FGIGVAGAKT NHSRDSVSNS
SATNVMDFPP ANNSDSLEFL LTYAVQHSNS SSGLPSFLPG LTPSAGRCLP LPTKLSYCNH
LGTKHFRVPN YLHHGSEEEV WAALHEWEGL LKSRCHRYLE WFLCLLLVPG CNASFPVTPP
PCRGFCEALK DLCWTHWKAG RLPISCESLP EEDGPYSCVF VNVSAENFSR EVGLLELIGD
PPPDQITKIY GPDKSPAYVF SPDANAGQVA RYHLPSPFYR DFSLLFYIQS TSDNAGVLFA
LTDASQSIIY VGVKLSEVKD GKQQIIFYYT EPGSQNSNVA ATFTVPSLVN LWTRFALSVR
DYNVVLYMDC EEFKMVHLER SSGKIELEEG AGLFVGQAGG ADPDKYQGII VELKIKDNPW
AAGYQCVEED DDCDTCGGSG SGLDIKQPPS EKESVIPLLS KLPVPPPVTS PAIAKKPVQL
EETEYTERPT YVPASGTKGE KGDPGEKGDR GPKGDPGTGV LSTNGDKGEK GSAGFGYPGS
KGQKGEPGTT GLPGPIGPPG PPGTIMRHSD GSTVEGPGAM GPPGLPGKDG QPGKDGEPGD
PGEDGKPGDV GPQGFPGTPG EPGLKGEKGE PSVGARGPPG PPGPPGKPGL SSKVDKLTFI
DMEGSGFGSE LESLRGPRGP PGPPGPPGVP GLPGQPGRFG TNGTDFPGLP GLPGVPGRNG
NSGIPGPPGP LGPPGKDGIP GQPGEKGAPG EPGEMGFPGA PGPEGNQGVP GFPGTPGEPG
LAGLPGPMGP RGLPGPPGPG IAAEFVDMEG SGFPLVSGGP GTRGPEGPPG LPGLPGLPGP
PGPKGDEGII GLPGLPGEKG YPGLPGLDGR PGLEGFPGPQ GQKGEEGSPG SKGEKGQDGI
GLPGPPGPPG QAVYLSSEDK TVPVLPGPEG PKGPKGDSGT PGLQGYPGLK GEKGEPGVVT
RPDGTILAAE AKGEKGEPGP SGPMGPGGPP GRYGRKGELG FPGRPGRPGM NGLKGEKGDP
ADLSGALGLR GPPGPPGPPG PPGSPVPVYE NNAFSDLGPP GPPGLPGYHG QKGEKGEQGL
PGPPGQFPYD LSRFSSTFRG ERGDKGDPGM KGEKGESGGG SNAAGLPGPQ GYPGLPGPKG
ESIRGLPGPP GPQGPPGAGF EGHPGPQGPP GPPGPPGPPS FPGPHRQHIS IPGPPGPPGP
PGPPGTSDPP SLGVRILATY QNLMSRAHEV PEGQLLFIRE REELYIRVHN GFRKILMEEK
ISIPGSGLDN EVYERSSSIH YSHGGTASSG SHRPFQPHLP VHARPEYSAY STAKPWRGDE
SIIDPHHLPE QPAVHPPRQG AQQESLDHFF PNNRQTETAP LAVHTHHDFQ PALHLIALNS
PQSGSMRGIR GADFQCFQQA RQVGLPGTFR AFLSSRLQDL YSIVRRADRS TVPIVNLRDE
VLFNNWENLF SGSEAPFRTG VRILSFDGRD VLRDSAWPQK YVWHGSDSKG RRLTESYCET
WRTDDTVVTG QASSLASSKL LEQKSNSCRN AFIVLCIENS FMTSSKK
//
