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Database: UniProt
Entry: A0A087X6Q2_POEFO
LinkDB: A0A087X6Q2_POEFO
Original site: A0A087X6Q2_POEFO 
ID   A0A087X6Q2_POEFO        Unreviewed;       972 AA.
AC   A0A087X6Q2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Trafficking protein, kinesin binding 2 {ECO:0000313|Ensembl:ENSPFOP00000001455.2};
GN   Name=TRAK2 {ECO:0000313|Ensembl:ENSPFOP00000001455.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000001455.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000001455.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the milton family.
CC       {ECO:0000256|ARBA:ARBA00007007}.
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DR   EMBL; AYCK01018607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A087X6Q2; -.
DR   STRING; 48698.ENSPFOP00000001455; -.
DR   Ensembl; ENSPFOT00000001458.2; ENSPFOP00000001455.2; ENSPFOG00000001467.2.
DR   eggNOG; KOG4360; Eukaryota.
DR   GeneTree; ENSGT00940000158202; -.
DR   OMA; LDGSHKF; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006933; HAP1_N.
DR   InterPro; IPR022154; TRAK1/2_C.
DR   PANTHER; PTHR15751; TRAFFICKING KINESIN-BINDING PROTEIN; 1.
DR   PANTHER; PTHR15751:SF13; TRAFFICKING KINESIN-BINDING PROTEIN 2; 1.
DR   Pfam; PF04849; HAP1_N; 1.
DR   Pfam; PF12448; Milton; 1.
DR   SMART; SM01424; HAP1_N; 1.
DR   SMART; SM01423; Milton; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT   DOMAIN          38..339
FT                   /note="HAP1 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01424"
FT   DOMAIN          399..544
FT                   /note="Trafficking kinesin-binding protein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01423"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          926..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          127..161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          189..332
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..837
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   972 AA;  106619 MW;  84F903D026A8BD8D CRC64;
     MFEAKPRTVE KKESSTETDE GLGSSGRHYT SSSLGSCSAG SGSLYLSDSQ DWVVSPSCSP
     DEPPTQISSI SPMLAEETLR YMILGANRVE QMTKTYNDIE VVTHLLAERD RDLELAARIG
     QSLLQRNHLL QERNDAVEEQ LAQAVDQVHQ LQHELNKKDE LLRIVASASE EGEQDPTVST
     PQQQPQAAAV AALGQLEQLQ NKLEELEEEN LALRSEACQL KRDTMTYEEK EQQLVSDCVK
     ELRESNSQMV SLTDELSQKN EELLRHQEEI AQLLSQIVEL QHRVKELALE KEELRIHLQA
     SKDAQRQLTA ELNELAERNA ECVEMLHESQ DEIRDLRSRS SPSSGMRRHL SYGLFPMESL
     AAEIEGSMRR ELSIDEETAF QDQRISLKRV FQTVRSVNAS ASRAALATPP IPGSGQSSLV
     MTAQPFQSAQ GQDIMTYPKS GCRDEVQMGK PGLPGGNDLT KALHRLSLRR QNFLSERQFF
     QAEREKKLQN QTGAEADGEG SDCSSPMGSV LSSFSNLSDL TVGSTVFKTF LPEKLQIVKP
     IEGSLTLHHW QQLAQPHLAT ILDPHPGVVT KGFRPLAQDA MFQLSDMEED EEAEEHRETA
     ALEKGTAEKG KEELDEEEEE CGITFNVRCS STPEDRNHPV APLPSIRSTS PGAPSTSSFV
     PSDLYLTPNH VTEKSNQLAL PIPGASTTTV QSQSRASTST TSSCVQNPGK SQSSTFSTYT
     FTTCRILHPT DITQVTPSSQ SSISANTPSS MRTGPSTPVT PCRLSLGDSF PPRRPPAPPC
     GLAKLVLERG ISAQVSTDVP SPLPRSAPRQ PLLRLMPSTP PNSPSHSPTP SPLPMEPRQH
     PSDNFLASRP AELFLQDVYG LNPGRDKANP PSVSLVERLR RLGFTKVLHN SESDTPVPHQ
     ESATFVSAGG GSLMDGLRRN QSLPAMIGAR AGSKSTGHPP HPTSLAIPPP PWGNLKERRR
     HLASISHPPR SS
//
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