ID A0A5J5DIJ3_9PERO Unreviewed; 866 AA.
AC A0A5J5DIJ3;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAA8593167.1};
GN ORFNames=FQN60_009283 {ECO:0000313|EMBL:KAA8593167.1};
OS Etheostoma spectabile (orangethroat darter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Etheostomatinae; Etheostoma.
OX NCBI_TaxID=54343 {ECO:0000313|EMBL:KAA8593167.1, ECO:0000313|Proteomes:UP000327493};
RN [1] {ECO:0000313|EMBL:KAA8593167.1, ECO:0000313|Proteomes:UP000327493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EspeVRDwgs_2016 {ECO:0000313|EMBL:KAA8593167.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA8593167.1};
RA Moran R.L., Catchen J.M., Fuller R.C.;
RT "A chromosome-level genome assembly, high-density linkage maps, and genome
RT scans reveal the genomic architecture of hybrid incompatibilities
RT underlying speciation via character displacement in darters (Percidae:
RT Etheostominae).";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
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:KAA8593167.1}.
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DR EMBL; VOFY01000004; KAA8593167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5DIJ3; -.
DR Proteomes; UP000327493; Chromosome 4.
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; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000327493}.
FT DOMAIN 533..579
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 692..860
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..300
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..640
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 92821 MW; F99B37DFB78F94E6 CRC64;
MLARALALAQ GAEPVETRAV QALATKERRE SPAPLGPPAP LALQGLQQSF QLALTARLLQ
ESRDPGDQLD RKVPRAPRDQ QELMESQAIQ GRTEKLVLMD LLASLEPRGT LELKERRDCL
AYQVPLVPPV LLVPLRASLV CRVLMAAQEC QVPREKRDLE ETLVYQELQE RADWLVCLDL
SDLLGHLGLL GLLDQAIGLD LMTWRALVEV SAMDCLASED LKEDRVLLAC LDFRVKLGCL
VSQGPKGSSG NKGDRGDPGR DGTGIPGPPG PPGPPGQIVY QTSGNVVGNA GPQGGPGLPG
QAGFPGPIGP KGDRGDAGLP GYGVKGEKGE PGLIIGPDGN LLHLEGLTGL KGDRGSPGPV
GLTGRPGVNG YKGEKGEAGV GSGYSYPGPV PGPPGPPGPP GPPGPAVPFD RFNQLKEKKE
SRVPEDFQNE LKGERGESGV KGEKGEPGGG YYDPRFGGVQ GSPGPPGKQG LQGPKGESIM
GPPGPQGPPG SPGIGYDGRP GPPGPPGPPG SPSLPLSVFL DLPVLLVHLE YQVTVLRSYD
TMVATARRQA EGSLIYIIDK ADLYLRVRDG LRQVMLGEYS PFFRDLDNEV AEFQPPPVIL
YPQDRTQNNG AGHYSQGGSG IRPIEPPPQP AVDPRYPPQY DPRFPDPRLT GQTDGRPATQ
WTENRYPVTP QRRPSPPVLQ PAGRADPSAS GLHLIALNAP QTGNMRGIRG ADFLCFQQAR
AIGLKGTFRA FLSSKLQDLY TIVRRSDRDS VPIVNLKDQE LFSSWQSLFD DEANKMRENV
PIYSFDGRDT LRDSAWPEKM VWHGSSNKGH RQTDDYCETW RAGDPAVTGL ASSLQSRHLL
QQTSSSCSGS YIVLCIENAL TTYSKK
//
