ID A0A6P9BWQ0_PANGU Unreviewed; 1846 AA.
AC A0A6P9BWQ0;
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_034276143.1};
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_034276143.1};
RN [1] {ECO:0000313|RefSeq:XP_034276143.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_034276143.1};
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}.
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DR RefSeq; XP_034276143.1; XM_034420252.2.
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_034276143.1};
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..1846
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028192825"
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..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1512
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 826..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..931
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1033
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1064
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1191
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1432
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1506
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 1846 AA; 192827 MW; CF8A17BD9DDEE4F6 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 GEKGELGVKG
SAGFGYPGSK GQKGEPGTTG LPGPIGPPGP PGTIMRHSDG STVEGPGAMG PPGLPGKDGQ
PGKDGEPGDP GEDGKPGDVG PQGFPGTPGE PGLKGEKGEP SVGARGPPGP PGPPGKPGLS
SKVDKLTFID MEGSGFGSEL ESLRGPRGPP GPPGPPGVPG LPGQPGRFGT NGTDFPGLPG
LPGVPGRNGN SGIPGPPGPL GPPGKDGIPG QPGEKGAPGE PGEMGFPGAP GPEGNQGVPG
FPGTPGEPGL AGLPGPMGPR GLPGPPGPGI AAEFVDMEGS GFPLVSGGPG TRGPEGPPGL
PGLPGLPGPP GPKGDEGIIG LPGLPGEKGY PGLPGLDGRP GLEGFPGPQG QKGEEGSPGS
KGEKGQDGIG LPGPPGPPGQ AVYLSSEDGP KGPKGDSGTP GLQGYPGLKG EKGEPGVVTR
PDGTILAAEA KGEKGEPGPS GPMGPGGPPG RYGRKGELGF PGRPGRPGMN GLKGEKGDPA
DLSGALGLRG PPGPPGPPGP PGSPVPVYEN NAFSDLGPPG PPGLPGYHGQ KGEKGEQGLP
GPPGQFPYDL SRFSSTFRGE RGDKGDPGMK GEKGESGGGS NAAGLPGPQG YPGLPGPKGE
SIRGLPGPPG PQGPPGAGFE GHPGPQGPPG PPGPPGPPSF PGPHRQHISI PGPPGPPGPP
GPPGTSDPPS LGVRILATYQ NLMSRAHEVP EGQLLFIRER EELYIRVHNG FRKILMEEKI
SIPGSGLDNE VYERSSSIHY SHGGTASSGS HRPFQPHLPV HARPEYSAYS TAKPWRGDES
IIDPHHLPEQ PAVHPPRQGA QQESLDHFFP NNRQTETAPL AVHTHHDFQP ALHLIALNSP
QSGSMRGIRG ADFQCFQQAR QVGLPGTFRA FLSSRLQDLY SIVRRADRST VPIVNLRDEV
LFNNWENLFS GSEAPFRTGV RILSFDGRDV LRDSAWPQKY VWHGSDSKGR RLTESYCETW
RTDDTVVTGQ ASSLASSKLL EQKSNSCRNA FIVLCIENSF MTSSKK
//
