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Database: UniProt
Entry: A0A3L8S6N9_CHLGU
LinkDB: A0A3L8S6N9_CHLGU
Original site: A0A3L8S6N9_CHLGU 
ID   A0A3L8S6N9_CHLGU        Unreviewed;      1419 AA.
AC   A0A3L8S6N9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=COKA1 protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DV515_00011707 {ECO:0000313|EMBL:RLV97492.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV97492.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV97492.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV97492.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV97492.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
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:RLV97492.1}.
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DR   EMBL; QUSF01000056; RLV97492.1; -; Genomic_DNA.
DR   STRING; 44316.ENSEGOP00005022780; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 5.
DR   CDD; cd01482; vWA_collagen_alphaI-XII-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24020:SF39; COLLAGEN ALPHA-1(XX) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   Pfam; PF00041; fn3; 5.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00060; FN3; 5.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 4.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          44..135
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          258..430
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          463..552
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          553..644
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          688..778
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          780..870
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          137..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1314
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1419 AA;  151321 MW;  804699BFF869F521 CRC64;
     MILPSRGMEA APLREVLLTM LIHTWFLLAC LPVVSHVWGR VGQGSGRLKL TVLSEDRLQM
     KWKETEGNIS GYKVRVKPMA GDSEQEVMLK TKTPKATVGG LSPTKEYTLQ VYVLNGSQEV
     LFAKRKFVIE ELRNASQTRN NRRNAGAVSG KNLTSSAAEH SGVAEATPPP LNTALAHSAK
     DRAEKKRQKG IQPKSSGETT RNQPSVEASV TEAASTTPKS SLHTPANTEQ ESPGKEKPPK
     DPLRRGSQFQ CNTPAMIDMV LLVDGSWSIG RNNFKLIKDF LSNLISPFSI AEDKIRVGLS
     QYSSDPRTEW ELSAYSTREQ VLEAVRNLRY KGGNTFTGLA LTHVLEQNLK PDAGARLEAE
     KLVILLTDGK SQDDANLAAQ TLKNLGIEIF AIGVKNADEA ELRQVASEPL ELTVYNVLDF
     PLLSSLLGKL TRVLCTRIKE RSHKETTGST VKDTPVNTGA QLSPTDLKIS AVTSKSMHLA
     WSPPLRPPTK YRVVYYPSKG GTPKEVVLEG AVSSVQLSNL TSHTEYLVSV IPVYDTAAGD
     GLRGVTSTLP LSSPRSLRVS ELSHNSLRLS WKAAQGATHY LVLCSAAPDG AEDYTAEVKV
     TQPEVLLEGL SPSTGYSVAV YAMYGEDASD PASIQETTLA LSPPRYLSFS ELSHASVRVS
     WEPAAPAVRA HHVTYVSSRG GNAGQVPPPR ALKVTELSGN SLRLQWEAVA ASDVVVYQIK
     WSTASGEKPQ ELSLAGNVAT AVLPGLQKNT DYKISIWAYY KDGARSDTVS VHHRTNSRSP
     PTNLFIDSET PSSLQVHWTP PDGRVQHYKI TYNPVSDAAA QQTIMAPGKS SSVTLQSLLP
     DRAYKVTISA IHYTGESQSS STTGRTACPT INSTEGSIRG FDMMEVFGLV EKEYSSIKGV
     AMEPFVFSGS RTFTLFRDIQ LTQRTRDVHQ FAIPPEHTIV FLLRLLPDTP KEPFAVWQVT
     DEDFQPLLGV NLDPSKKSLT YFNHDYKADL QEVSFDEQEV KKIFFGSFHK VHVAVSHFKV
     KLYVDCKKTA EKPINTLGSI SSAGFIMLGK VSRTRGPRSG SVPFQLQTLQ ILCSSVGAEQ
     DRCCDLPALR DEDTCPTLAP ACSCTSGRPG LPGPPGPPGS PGRRGPQGEQ GEPGPKGEPG
     PPGQVGPAGP SGQQGSPGSQ GITVQGPVGP PGIKGEKGDT GIPGMQGMPG VQGAPGRDGL
     QGAKGVRGLE GTAGPPGPPG PRGFQGATGT RGSSGEKGPP GDVGPTGLPG PKGERGEKGE
     PQSLATIYQL VSQASHVLKF DSFIHEHARK PVPIWEERLK PGEPGPPGPP GPPGNSGERG
     ENGTPGQPGK DGYPGERGAP GPKGEKGMSG ASEEGSQGPR GRAGPPGEVV QGKPGPKGFP
     GNAGPPGFPG VRGQPGQPGH PGGCDISGCY EADRRDFVP
//
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