ID K7BUN1_PANTR Unreviewed; 1339 AA.
AC K7BUN1; A0A2J8M8R5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 28-JAN-2026, entry version 64.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSPTRP00000092192.1};
DE SubName: Full=Collagen, type XVIII, alpha 1 {ECO:0000313|EMBL:JAA17789.1};
GN Name=COL18A1 {ECO:0000313|EMBL:JAA17789.1,
GN ECO:0000313|Ensembl:ENSPTRP00000092192.1,
GN ECO:0000313|VGNC:VGNC:10689};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA17789.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000092192.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000092192.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136134; DOI=10.1038/nature04101;
RA Hughes J.F., Skaletsky H., Pyntikova T., Minx P.J., Graves T., Rozen S.,
RA Wilson R.K., Page D.C.;
RT "Conservation of Y-linked genes during human evolution revealed by
RT comparative sequencing in chimpanzee.";
RL Nature 437:100-103(2005).
RN [3] {ECO:0000313|EMBL:JAA17789.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Smooth vascular {ECO:0000313|EMBL:JAA17789.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSPTRP00000092192.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-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 EMBL; AACZ04000578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04000579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04000580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04068940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABF01004356; JAA17789.1; -; mRNA.
DR Ensembl; ENSPTRT00000098662.1; ENSPTRP00000092192.1; ENSPTRG00000014005.6.
DR VGNC; VGNC:10689; COL18A1.
DR GeneTree; ENSGT00940000158212; -.
DR OMA; VQDQHQN; -.
DR Proteomes; UP000002277; Chromosome 21.
DR Bgee; ENSPTRG00000014005; Expressed in liver and 21 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-ARBA.
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; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 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 2: Evidence at transcript level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:JAA17789.1};
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:UP000002277};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1339
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015095871"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 230..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..431
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..527
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..650
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..738
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..758
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 135889 MW; 32FD0868ACE13E2E CRC64;
MAPRCPWPWP RRRRLLDVLA PLVLLLGVRA ASAEPERVSE EVGLLQLLGD PPPQQVTQTD
DPDVGLAYVF GPDANSGQVA RYHFPSLFFR DFSLLFHIRP ATEGPGVLFA ITDSAQAVVL
LGVKLSGVQD GHQDISLLYT EPGAGQTHTA ASFRLPAFVG QWTHLALSVA GGFVALYVDC
EEFQRMPLAR SSQGLELEPG AGLFVAQAGG ADPDKFQGVI AELKVRRDPQ VSPMHCLDEE
GDDSDGASGD SGSGLGDTRE LLREETGVAL KPRLPTPPPV TTPPLAGGSS TEDSRSEEIE
EQTTVASLGA QTLPGSDSVS TWDGSVRTPG GRVKEGGLKG QKGEPGVPGP PGRAGPPGSP
CLPGPPGLPC PVSPLGPAGP ALQPVPGPQG PPGPPGRDGT PGRDGEPGDP GEDGKPGDTG
PQGFPGTPGD VGPKGDKGDP GVGERGPPGP QGPPGPPGPS FRHDKLTFID MEGSGFGGDL
EALRGPRGFP GPPGPPGVPG LPGEPGRFGV NSSDVPGPAG LPGVPGREGP PGFPGLPGPP
GPPGREGPPG RTGQKGSLGE AGAPGHKGSK GDPGPAGARG ESGLAGAPGP AGPPGPPGPP
GPPGPGLPAG FDDMEGSGGP FWSTARSAAG PQGPPGLPGL KGDPGVPGLP GAKGEVGADG
VPGFPGLPGR EGIAGPQGPK GDRGSQGEKG DPGKDGVGQP GLPGPPGPPG PVVYVSEQDG
SVLSVPGPEG RPGFAGFPGP AGPKGNLGSK GEQGSPGPKG EKGEPGSIFS PDGGALGPAQ
KGAKGEPGFR GPPGPYGRPG YKGEIGFPGR PGRPGMNGLK GEKGEPGDAS LGFGMRGMPG
PPGPPGPPGP PGTPVYDSNV FAESSRPGPP GLPGNQGPPG PKGAKGEVGP PGPPGQFPFD
FLQLEAEMKG EKGDRGDAGQ KGERGEPGGG GFFSSSLPGP PGPPGPRGYP GIPGPKGESI
RGQPGPPGPQ GPPGIGYEGR QGPPGPPGPP GPPGPPSFPG PHRQTISVPG PPGPPGPPGP
PGTMGASSGV RLWATRQAML GQVHEVPEGW LIFVAEQEEL YVRVRNGFRK VQLEARTPLP
RGTDNEVAAL QPPVVQLHDS NPYPRREHPH PTARPWRADD ILASPPRLPE PQPYPGAPHH
SSYVHLRPAR PTSPPAHTHR DFQPVLHLVA LNSPLSGSMR GIRGADFQCF QQARAVGLAG
TFRAFLSSRL QDLYSIVRRA DRTAVPIVNL KDELLFPSWE ALFSGSEGPL KPGARIFSFD
GKDVLRHPTW PQKSVWHGSD PNGRRLTESY CETWRTEAPS ATGQASSLLG GRLLGQSAVS
CHHAYIVLCI ENSFMTASK
//
