ID A0A286ZIL9_PIG Unreviewed; 1755 AA.
AC A0A286ZIL9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSSSCP00000031327.2};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSSSCP00000031327.2,
GN ECO:0000313|VGNC:VGNC:86869};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000031327.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000031327.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000031327.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000031327.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR SMR; A0A286ZIL9; -.
DR STRING; 9823.ENSSSCP00000031327; -.
DR Ensembl; ENSSSCT00000045242.3; ENSSSCP00000031327.2; ENSSSCG00000038089.3.
DR VGNC; VGNC:86869; COL18A1.
DR GeneTree; ENSGT00940000158212; -.
DR InParanoid; A0A286ZIL9; -.
DR Reactome; R-SSC-1442490; Collagen degradation.
DR Reactome; R-SSC-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-SSC-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-SSC-216083; Integrin cell surface interactions.
DR Reactome; R-SSC-8948216; Collagen chain trimerization.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000038089; Expressed in liver and 39 other cell types or tissues.
DR ExpressionAtlas; A0A286ZIL9; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030903; P:notochord development; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd07455; CRD_Collagen_XVIII; 1.
DR CDD; cd00247; Endostatin-like; 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; IPR035523; Collagen_XVIII_Fz.
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; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 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 Pfam; PF13385; Laminin_G_3; 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 1: Evidence at protein level;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZIL9};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1755
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023863378"
FT DOMAIN 340..456
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 44..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1024
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 355..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1755 AA; 178614 MW; CAA055A0F9FDB6EE CRC64;
MAPDPSGRPG HLGLLLLLAC CLAATWADPF PWLWFSEATM PKATPASVPQ ATPAPVPPGS
SPEQRPETPP RTWTPGMAPP TRGKPRPALS LVWRGWRGAR ARAPLSPRPP REPGPQGGEH
RGCGSQDPER GSGHPALHPA VGRHHAPREL RRRGDASPPT PTDPLTTPGP SSTLWESGTT
LWLSSGAPSS PDTQRTEAGT QPLPTQPPPS PGGPLAPFRA PSVPPPAPGR ASLSPAPGGA
PPWGSQLSPG WSQELDGKGL LPVAARPGQQ HRHPDVRRPP LLPLVTGSPG AHGPSALSSG
APATLSYVAL AALIGDGGAW LPHVANSSGP GLAHTSAQLG ATGRCLPLPP SLAICSRLGI
GRVWLPNHLH HGSGEEVQAA ARAWGALLQT RCHRFLAWFF CLLLAPPCGL GPAAPPPCRQ
FCETLEDACW SHLDGGGLPV PCASLPARED GHCVFIGPAA EGEAVEVGLQ QMLGEPLPRQ
VALVHDPDVG PAYEFDGISG VGQAALSLVP RTFFHDFSLL MRVRPASAGA GVLFAVTDAA
QAVVLVGVKL AAARGGQQQV QLLYTEPGAT RTRTAASFTL PALHGRWTHL ALSVDGAHVA
LFVDCEEVQL EPLSRSLRAL QLEPDARLFV AQAGRADPDK FQGMISELRV RGDPQVSPLQ
CRYGDEDEDD SDNEASGDLG SGLAEEAGER LGAPSGAPLR PRLPEAPPVT SPPLAGAGDE
EDSRTEEVEE ATTVPSPGAQ TLPGSGAVTT WDGSSWSPGD SLEERGLKGQ EEPGAQGLPG
QASPQGPTGP VMRSPEAQPV PGPQGPPGPP GPPGKDGAPG RDGEPGDPGE DGKPGDTGPQ
GFPGTPGDVG PKGEKGDPGV GPRGPPGPQG PPGPPGPSFR HDKLTFIDME GSGFGGDLES
LRGPRGFPGP PGPPGVPGLP GEPGRFGMNS SDVPGPAGLP GVPGRDGAPG PPGPPGPPGF
PGRDGQAGQT GQKGSVGEVG APGPKGSKGD PGPVGAPGNP GLAGVPGPAG PPGPPGPPGP
PGPGLAAGFD DMEGSGGPFW WAAQGADRPQ APPGPPGVKG DPGAVGPAGT KGEVGADGAP
GLPGLPGREG AAGPQGPKGE KGTRGDKGDP GKDGVGQPGL PGPPGPPGPV VYVSDRAVAS
VPGPEGRTGF AGFPGPAGPK GDLGSKGQPG LPGPKGEKGE PGTVFSPDGR PLTPAQKGAK
GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP GMNGLKGEKG EPGDASVGFS LRGPPGPPGP
PGPPGPAGTP VYDSNAFVES GRPGPPGLPG YQGPPGPKGD KGEMGPPGPP GQFPFDLLHM
EAELKGEKGD RGEAGQKGER GEPGGGGFFG SSVPGPPGPP GYPGIPGPKG ESIRGQPGPP
GPQGPPGIGY EGRQGPPGPP GPPGPPGPPS FPGPYRQTIS VPGPPGPPGP PGPPGSMGGS
SGVRVWATYQ TMLDKVPEVP EGWLMFVAER EELYVRVRNG FRKVLLEART PLPRGTGTDN
EVAALQPPVV QLHEGNPYPR REPPQPTARA WRGDDIRASP PRLPVAQPYP GAPHHGAYVH
PRPVHPTGSP AHTHHDFQPV LHLVALNSPQ SGGLRGIRGA DFQCFQQARA VGLAGTFRAF
LSSRLQDLYS IVRRADRAAV PIVNLRDEVL FPSWEALFSG SEGQLKPGAR IFSFDGRDVL
QHPAWPQKSV WHGSDPSGRR LTESYCETWR TEARTATGQA SSLLAGRLLE QKAAGCHHAF
IVLCIENSFM TSASK
//
