ID A0A9Q1J7W7_SYNKA Unreviewed; 734 AA.
AC A0A9Q1J7W7;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=SKAU_G00054290 {ECO:0000313|EMBL:KAJ8374849.1};
OS Synaphobranchus kaupii (Kaup's arrowtooth eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Synaphobranchidae;
OC Synaphobranchus.
OX NCBI_TaxID=118154 {ECO:0000313|EMBL:KAJ8374849.1, ECO:0000313|Proteomes:UP001152622};
RN [1] {ECO:0000313|EMBL:KAJ8374849.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WJC10195 {ECO:0000313|EMBL:KAJ8374849.1};
RX PubMed=36758078;
RA Parey E., Louis A., Montfort J., Bouchez O., Roques C., Iampietro C.,
RA Lluch J., Castinel A., Donnadieu C., Desvignes T., Floi Bucao C.,
RA Jouanno E., Wen M., Mejri S., Dirks R., Jansen H., Henkel C., Chen W.J.,
RA Zahm M., Cabau C., Klopp C., Thompson A.W., Robinson-Rechavi M.,
RA Braasch I., Lecointre G., Bobe J., Postlethwait J.H., Berthelot C.,
RA Roest Crollius H., Guiguen Y.;
RT "Genome structures resolve the early diversification of teleost fishes.";
RL Science 379:572-575(2023).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAJ8374849.1}.
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DR EMBL; JAINUF010000002; KAJ8374849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q1J7W7; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP001152622; Chromosome 2.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; 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; 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:SF1077; COLLAGEN ALPHA-3(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
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:UP001152622}.
FT DOMAIN 463..510
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 559..728
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..181
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 74578 MW; BAF9EF22044F704D CRC64;
MGDPGLPGPI GPEGPTGPVG LHGPPGPPGP PGPSGLGFAL EMEDLEGSGR LGAFGTLGPE
GPQGPPGLPG LPGPKGADGA PGVGEKGERG DPGREGNPGV AGLPGLRGET GENGGPGAKG
ERGADGLSVP GPPGPPGPPG PIVSLQDLLL NDTDGTFNFT DTQGPPGPMG PEGLPGRAGF
PGPRGPKGDT GPQGIQGPTG LKGEKGESGV TIAADGSLMT RLRGPQGPNG FKGERGFPGP
VGLMGPIGPQ GPKGEFGFPG RPGRPGMVGK KGDRGDSVSQ PGAPGPPGPP GRPGPLNCPK
GTVFPVPPRP HCKTPINGNT DSTPGSDCRG RIRAKGEKGE AGFPGFPGSM DSWLPEGVAG
DKGDAGYRGE KGQKGEAGIP GSPGLPGRSG LVGPKGEAVV GPQGPPGNSG LPGHPGYGRP
GPQGPQGPPG PPGPPPLFGS AVAIPGPPGP PGLPGASGLG NPVTTYKTVE TLFQHMHRSA
EGTMAYVSEK SELYIRVREG WRKVQLGELV SLPANSPTQV SHVLSRPGEV SYSDLITQGQ
VYLPGYNILA HTIHTGPGLH LVALNAPFSG DMRGIHGADY QCYQQARAMG LVTTYRAFLS
SPLQDLATIV KKGDRFNMPI LNLKGEVLFN NWMSIFSGNG GVFQPSIPIY SFDGRNVITD
PSWPQKMVWH GSSAVGTRLT SNFCEAWRAG HMAVTGQASL LHSGRLLGQH TRSCSNHFIV
LCIENTYVQD AYRN
//
