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Database: UniProt
Entry: A0A6I8MZA9_ORNAN
LinkDB: A0A6I8MZA9_ORNAN
Original site: A0A6I8MZA9_ORNAN 
ID   A0A6I8MZA9_ORNAN        Unreviewed;      1342 AA.
AC   A0A6I8MZA9;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSOANP00000034019.1};
GN   Name=COL18A1 {ECO:0000313|Ensembl:ENSOANP00000034019.1};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000034019.1, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000034019.1, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000034019.1,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000034019.1}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000034019.1};
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSOANP00000034019.1}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000034019.1};
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_039768565.1; XM_039912631.1.
DR   Ensembl; ENSOANT00000063071.1; ENSOANP00000034019.1; ENSOANG00000043147.1.
DR   GeneID; 120638499; -.
DR   CTD; 80781; -.
DR   GeneTree; ENSGT00940000158212; -.
DR   Proteomes; UP000002279; Chromosome 7.
DR   Bgee; ENSOANG00000043147; Expressed in liver and 8 other cell types or tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 3.
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   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
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:UP000002279};
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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1342
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5026136946"
FT   DOMAIN          30..218
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          222..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..459
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..501
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..545
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..611
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..682
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..700
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..837
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..982
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1006
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1342 AA;  137804 MW;  BFD5B353D47C0178 CRC64;
     MPARWPLLLA GLLAFLPLSA AQDPENFSNE VGLLQLIGEP PPKQITQVYD AATGLGYVFG
     PDANSGQVAR YYVPNPFYKD FSLIFHVKPT TDGPGMLFAL TDATQSLIFV GVKLSKATDG
     KQRVIFYYTE PGSESSVVAA RFRQPLPARQ WNRFAVGVEN MEAVLYVNCQ EVERVSFERS
     PDDLVLEAGS GLFVAHAGGA DPDKFQGVIA ELKVRGDPQV TSLQCLDDDD DDDSDGSSGD
     YGSGLEDKQD HPRREPASPL IPDLPEAPPV TSPPLAGTAV QEEGESEADS QPGQLEEEEG
     NLASSGGQSH PKGDKEKKVE HGPEGSEGNL EEVGKSQENL GFGHASTKGQ KGEPGARGEP
     GPMGPQGPAG SVLQGPGDPN VEQVSGPQGP PGPTGSPGID GSPGKDGEPG VPGEDGKPGD
     IGPQGFPGTP GDIGPKGDKG DPGVGPRGPP GPPGPPGPPG SSSKTDKLTF IDMEGSGFGG
     DLESLRGPRG FPGPPGPPGV PGLPGEPGRF GTNGTDTPGP PGLPGLPGRD GAPGPQGPPG
     PPGPPGKVGN QGEMGLKGED GVIGLPGAPG LKGSKGEDGP VGKPGEAGAV GQPGPIGPPG
     QPGPPGPPGL PAPGFGAGFD DMEGSGIPFL TGGPQGPPGL PGLKGDDGIP GIAGPPGEKG
     DHGAPGLPGQ PGMEGPEGPQ GSKGDKGSPG EKGEPGKDGV GHPGLPGPPG PPGRMVYVSP
     EYGSTGPKGD LGTKGYWGTP GPKGEKGEPG MVVGSDGMVL APGQKGNKGD PGFRGPPGPY
     GRPGHKGEIG FPGRPGRPGM NGLKGEKGEP ADVSGGFGFR GLPGLPGPPG PPGPPGASVP
     LYDSNAFGET GPAGPPGLPG FPGTPGQKGE KGDIGPAGPP GPFPYDFSHF GTSVKGEKGA
     RGDAGQKGER GEPGSGGFFG SSAAGPPGPP GPQGYPGIPG PKGDSIRGQP GPPGPQGPPG
     IGYEGRQGPP GPPGPPGPPS FPGPHRQTIT VPGPPGPPGP PGPPGTTGPS SGQLRILSTY
     QAMLNKAREL PEGWVIFVAD REELYVRVRN GIRKIMLEAQ IPLPQGSENE VAVVQPPVFQ
     YPQSGSQFND GNNPYPRREH PYSTAKPWRS DDILPGYPRY PDQSNSRHNY HGAQHHQEHQ
     HSLYPNLRPQ YPIPSAVHTH HDFQPALHLI ALNTPLSGSM RGIRGADFQC FQQAREVGLT
     GTFRAFLSSR LQDLYSIVRR ADRNGVPIVN LKDELLFNNW EALFSGSEGQ LKPGSRIFSF
     DGKDVLRHSS WPQKSVWHGS DSKGRRLTEN YCETWRTDEA MVTGQASSLM SGKLLEQKPM
     SCRNAFVVLC IENSFMTSLS KK
//
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