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Database: UniProt
Entry: A0A9L0IBA9_EQUAS
LinkDB: A0A9L0IBA9_EQUAS
Original site: A0A9L0IBA9_EQUAS 
ID   A0A9L0IBA9_EQUAS        Unreviewed;      1109 AA.
AC   A0A9L0IBA9;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 13.
DE   SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSEASP00005037491.1};
GN   Name=COL18A1 {ECO:0000313|Ensembl:ENSEASP00005037491.1};
OS   Equus asinus (Donkey) (Equus africanus asinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005037491.1, ECO:0000313|Proteomes:UP000694387};
RN   [1] {ECO:0000313|Ensembl:ENSEASP00005037491.1, ECO:0000313|Proteomes:UP000694387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=33293529;
RA   Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X.,
RA   Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang,
RA   C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li,
RA   J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G.,
RA   Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G.,
RA   Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li,
RA   S., Zhou, X. and Zhong, J.;
RT   "Donkey genomes provide new insights into domestication and selection for
RT   coat color.";
RL   Nat. Commun. 11:6014-6014(2020).
RN   [2] {ECO:0000313|Ensembl:ENSEASP00005037491.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSEASP00005037491.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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DR   AlphaFoldDB; A0A9L0IBA9; -.
DR   Ensembl; ENSEAST00005075548.1; ENSEASP00005037491.1; ENSEASG00005038430.1.
DR   GeneTree; ENSGT00940000158212; -.
DR   Proteomes; UP000694387; Chromosome 18.
DR   GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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   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; IPR016187; CTDL_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694387}.
FT   DOMAIN          799..847
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          935..1104
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          1..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..29
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..164
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..229
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..268
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..296
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..312
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..354
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..377
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..438
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..483
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..510
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..530
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..623
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..722
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..768
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..790
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1109 AA;  111349 MW;  3C9EDDEA5A354EA2 CRC64;
     MIAELRVRAD PHVSPVHCLE DDDDDDDGAS GDFGSGLEEP RERLGEEPGT SLTLGLPDAP
     PVTSPPLAGS SDVEDSRTEE IEEETTVSSI GAHTLPGSDP AATWDGSAWS PGGSLREGGL
     KGQKGEPGLP GPVGPQGPAG PAMHSPDAQP IPGPQGPPGP PGPPGKDGAP GRDGEPGDPG
     EDGKPGDTGP QGFPGTPGDV GPKGEKGDPG VGPRGPPGPQ GPPGPPGPSF RPDKLTFIDM
     EGSGFGGDLE TLRGPRGFPG PPGPPGVPGL PGEPGRFGMN SSDVPGPAGL PGVPGRQGPP
     GLPGPPGPPG PPGRDGRPGG TGQKGSLGEA GPPGPKGSKG DPGPIGAPGE NGLAGPPGPA
     GPPGPPGPPG LPGPPGPGLA AGFDDMEGSG GPFWSTARGA DGPQGLPGLP GVKGDPGPAG
     PPGTKGEVGA DGGPGFPGLP GREGAAGAQG PKGEKGTQGE KGDPGKDGVG QPGLPGPPGP
     PGPVVYVSEQ DRAVASVPGP EGRPGFAGFP GPAGPKGDLG SKGQQGLPGP KGEKGEPGAV
     FGPDGGVLTA SQKGAKGEPG FRGPPGPYGR PGHKGEIGFP GRPGRPGMNG LKGEKGEPGD
     ASVRFGMRGL PGPPGPPGPP GLPGTPVYDT NAFLESGRPG PPGLPGHQGP SGPKGDKGEV
     GPPGPPGQFP LDLLQLEAEM KGEKGDRGPA GQKGERGEPG AGGFFGSSVP GPPGPPGYPG
     IPGPKGESIR GQPGPPGPQG PPGIGYEGRQ GPPGPPGPPG PPGPPSFPGP YRQTISVPGP
     PGPPGPPGPP GTMGTSSGVR IWATYQTMLD KVPEVPEGWL IFVAEREELY VRVRNGFRRV
     LLDARMPLPH GTDNEVAALQ PPVVQLHEGN PYPRREVPHS TARPWRADDI LASPPRLPDP
     QPYPGAPHHG SYVHLRPARP TSSLTHTHQD FQPVLHLIAL NSPQSGGLRG IRGADFQCFQ
     QARAVGLAGT FRAFLSSRLQ DLYSIVRRAD RASVPIVNLR DEVLFPNWEA LFTGSEGRLK
     PGARIFSFDG RDVLQHPAWP QKSVWHGSDP SGRRLTESYC ETWRTEATAA TGQASSLLAG
     RLLEQKSASC HNAFIVLCIE NSFMTSSSK
//
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