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Database: UniProt
Entry: A0A8C3UXS1_CATUS
LinkDB: A0A8C3UXS1_CATUS
Original site: A0A8C3UXS1_CATUS 
ID   A0A8C3UXS1_CATUS        Unreviewed;       862 AA.
AC   A0A8C3UXS1;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 20.
DE   RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0008006|Google:ProtNLM};
GN   Name=LOC117006265 {ECO:0000313|Ensembl:ENSCUSP00005021002.1};
OS   Catharus ustulatus (Russet-backed thrush) (Hylocichla ustulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Turdidae; Catharus.
OX   NCBI_TaxID=91951 {ECO:0000313|Ensembl:ENSCUSP00005021002.1, ECO:0000313|Proteomes:UP000694563};
RN   [1] {ECO:0000313|Ensembl:ENSCUSP00005021002.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Delmore K., Vafadar M., Formenti G., Chow W., Pelan S., Howe K., Rhie A.,
RA   Mountcastle J., Haase B., Fedrigo O., Jarvis E.D.;
RT   "Catharus ustulatus (Swainson's thrush) genome, bCatUst1, primary haplotype
RT   v2.";
RL   Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCUSP00005021002.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSCUSP00005021002.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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DR   AlphaFoldDB; A0A8C3UXS1; -.
DR   Ensembl; ENSCUST00005021771.1; ENSCUSP00005021002.1; ENSCUSG00005013380.1.
DR   Proteomes; UP000694563; Chromosome 23.
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   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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:SF1114; COLLAGEN ALPHA-1(XVIII) 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:UP000694563}.
FT   DOMAIN          583..626
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          691..856
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          78..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..175
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..211
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..276
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..286
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..306
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..321
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..349
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..406
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..532
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   862 AA;  88587 MW;  83157DA60D453C42 CRC64;
     MAFPAPQIPA PQQGGGTWRV MCGVPGCRAA GGTAVAVGGA GNWECCGTLV PLQPCHFPSQ
     LSFAPADRDA SVGKVLLSKP PLATAPRRRD QLSRGTAKGS DHAPPRTRGQ HRPTAAPEIF
     EGSAVEEEFL QIQTTAKGLP RRVPSAPETD PALQMHNISG CVCPVRPGPP GPPGPKGDKG
     DRGFPGERGQ PGFSGEKGKS GSPGQPGHQG PRGPPGPPGP PGPPGPPGAW GGRGQPAPAA
     LPERSENEHL GVSSPVGNPG PPGPPGLPGM PGPPGYPGHD GPQGAPGREG KPGPPGPPGA
     VGPPGFPGAE GLPGSPGSAG PDGPPGAPGL PGPQGPPGVP GHEGPPGPPG SASLPGKPGL
     RGEPGFPGPK GEKGEYGLPG MPGSPGRTGE PGSPGMPGPM GPPGPPGDYR VSRGSLAVGP
     RQGAPQCHPH ILSLQCDSRH AGHRGLAGPM GPKGEKGDPG EPGCCYGEHG CKPGHLPFPS
     TGSQPGSWGS IHRFQTDSKE EPEIYGAIIP HGLRGPPGNP GPPGPPGPPG PPGLLYLNRV
     HPVHAQPPCK QPAPADRSWP SDAGVPHTEP SDSRGDLQRQ TWVFKSKELM VKASSAVPEG
     SLVYVREGSN AFLRTPTGWS RLLLEDPKSF LAGDDPSAST PQYQEAKRAQ PRGSNILSPM
     QSPTDSLIQK EEEQGLPQIL PTTIAPRIPS LRLAALNVPL SGDMSGIRGA DLQCYRQSQE
     AGLYGTFRAF LSSPTQHLVS IVKRTDRTLP IVNLKGQLLA KSWSSLFGGQ SGAALQGPIY
     SFNGRNILLD PLWPRRLAWH GSTPRGGHAR RWDCQGWRSS GTAEGVATAL GEGRLLAGQR
     HNCSTPLAVL CIEVAFPYRH MW
//
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