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Database: UniProt
Entry: M4A742_XIPMA
LinkDB: M4A742_XIPMA
Original site: M4A742_XIPMA 
ID   M4A742_XIPMA            Unreviewed;      1516 AA.
AC   M4A742;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Nuclear receptor coactivator {ECO:0000256|PIRNR:PIRNR038181};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000010286.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000010286.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000010286.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR038181}.
CC   -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC       family. {ECO:0000256|ARBA:ARBA00009933, ECO:0000256|PIRNR:PIRNR038181}.
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DR   STRING; 8083.ENSXMAP00000010286; -.
DR   Ensembl; ENSXMAT00000010300.2; ENSXMAP00000010286.2; ENSXMAG00000010250.2.
DR   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00950000183021; -.
DR   HOGENOM; CLU_001988_0_0_1; -.
DR   InParanoid; M4A742; -.
DR   OMA; PIMPNAQ; -.
DR   OrthoDB; 4230728at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016922; F:nuclear receptor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd18950; bHLH-PAS_NCoA2_SRC2; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   Gene3D; 6.10.140.20; Nuclear receptor coactivator, Ncoa-type, interlocking domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR010011; NCO_DUF1518.
DR   InterPro; IPR032565; NCOA2/3_DUF4927.
DR   InterPro; IPR028822; NCOA2_bHLH.
DR   InterPro; IPR009110; Nuc_rcpt_coact.
DR   InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR   InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR   InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR014935; SRC/p160_LXXLL.
DR   PANTHER; PTHR10684; NUCLEAR RECEPTOR COACTIVATOR; 1.
DR   PANTHER; PTHR10684:SF2; NUCLEAR RECEPTOR COACTIVATOR 2; 1.
DR   Pfam; PF07469; DUF1518; 2.
DR   Pfam; PF16279; DUF4927; 1.
DR   Pfam; PF16665; NCOA_u2; 1.
DR   Pfam; PF08815; Nuc_rec_co-act; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF14598; PAS_11; 1.
DR   Pfam; PF08832; SRC-1; 1.
DR   PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR   SMART; SM01151; DUF1518; 2.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR038181};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038181};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR038181};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR038181}.
FT   DOMAIN          28..85
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   DOMAIN          121..185
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1255..1374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1393..1516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          75..105
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        12..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1258..1284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1299..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1330..1347
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1516 AA;  163530 MW;  61C8B3F0FAF50FC1 CRC64;
     MMSGVGENSS DPARAEARKR KECSAELIGP SPKRSNEKRN REHENKYIEE LAELIFANFN
     DIDNFNVKPD KCAILKETVK QIRQIKEQEK AAAANEEEVQ KADVSSTGQS VIDKDALGPM
     MLEALDGFFF VVNMEGNIVF VSENVTQYLR YNQEELMNTS VYSVLHVGDH AEFIKNLLPK
     SLVNGVPWSS EGPRRNSHTF NCRMLVNPHS ENQDESHEPQ QQKYETMQCF AVSEPKSIKE
     EGDDFQSCLI CVARRVPTKE RPMLPTHESF TTRQDLQGKI TSLDTSLLRA SMKPGWEDLV
     RRCIQRFHLQ NDGEMSFAKR HQQEVLRHGQ AFSPIYRFSL SDGTIVSAHT KSKLVRSSAT
     NEPQLYMSLH LLQREHPVCG MGQDIGGQET GMTPKPMNPS MTPPTPCSLP GLGLQGQDTT
     ISSNSTPFSP PGPAGPREPA AMGGHMQGYR FGCPPPHPNY TGGMQPPQQG PNWRMNSPSR
     ASPSPAGGPH PAQQNSMLSP RHRGSPGGAG SPRVAGGLQS PSPVGMCGSG PGSAGSTHSN
     SYTSSSLSAL QALSECHGVG HGPSHAHTLG SPDRKIGSPA GVTPGSGVNP HMMSKFGGSS
     SNAGGAGDFS SHSEVNQGHA EGNQTEPKEE REGSLDGHDS HDAHSRVHDN KGNTKLLQLL
     TTKPEPLETP LSPGGGGEGK DQAGAGVRGG HAVGNTHATS LKEKHKILHQ LLQNSTSPVD
     LAKLTAEATG KELGQDQSQG AGNQSSGAEI TPKQEPLSPK KKDNALLRYL LDKDDTVMKD
     KVSKLEPGEV KVKEHPQVKV EKQDAGYDRA EQSSELDDIL NDLQSAQPQL FCEQRPVSLP
     SPMDKQNIFN DILQMSENNA AMATQQQPRG LGMGQTNFGV VRPGQPGRAL PVRSVSLDMN
     VPSQQPSLQY PIRANSPYPV MQQQQGMLGG HGMMPNQPGM GNAGLMTQGG PRPAMQQQQQ
     QQSEGWTGPA SAPPIGASAP GQQGGMQGRM VPGTAPMRPN SQPGPRPMLQ SPLMANAQPD
     MDINMVGHHF SQQQAPPNQT APWPDSMMPI DQTPFVNQNR PAQQDDLLCN PSLDQGSAVD
     EGALMSQLYS ALKDFDGLEE IDRALGIPAL VEQSQSLEPD QFPQDSTIML DQKPPMYTQQ
     FGPPPSHMVP RGFPGPPMQE PGFHLMAGQM GPRPTYPMMR MQPRPGLRPG GVAPNQPNAL
     RLQLQHRLQS QQQKSQPMMT QMTGVSNVNL PLRASAPSQG NINAHMLAQR QREMLSNHLR
     QRQQQQQQHV QQAQQVQQQR SIAMRAQGLG LPPNMAGGMS NPRNPQAAPQ QFPYPPSYGT
     STGLASSPPP TSPFSSPLSP SLPSLPPNPQ LHLHGTSSSS TSSSSSQMMM GNTNMMGGQY
     VGVLNPQMQH SAFQFPNSGM SQQADGSFAG GSTPQSPLLS PRMAHTQSPM MQQGQQNAAF
     QGSPDMNGWP QGNMGGNSMF SQQQASPQFT QQNSGNMYNG NGMGLNNQLS SQMSVTSMAS
     GSSPGLPSMG QEQKFC
//
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