ID A0A2U9BIN1_SCOMX Unreviewed; 1413 AA.
AC A0A2U9BIN1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Putative rab effector MyRIP-like isoform 2 {ECO:0000313|EMBL:AWP03837.1};
GN ORFNames=SMAX5B_006220 {ECO:0000313|EMBL:AWP03837.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP03837.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP03837.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP026249; AWP03837.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000026175; -.
DR Proteomes; UP000246464; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR006788; Myrip/Melanophilin.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14555; MYELIN-ASSOCIATED OLIGODENDROCYTIC BASIC PROTEIN MOBP -RELATED; 1.
DR PANTHER; PTHR14555:SF6; RAB EFFECTOR MYRIP; 1.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF04698; Rab_eff_C; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 4..124
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT REGION 417..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..49
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 668..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1413 AA; 160294 MW; 2B7835BA4E4A9C3C CRC64;
MGRKLDLSGL TDNEAEHVLQ VVQRDMKLRK KEEKRLSELK QELDEEGSRC LLLSRQSCFN
QRCCIRCCLP FTFLLNPKRQ CRDCRYNVCK ACRLYNKQDK AWVCSACQKS RLLKTQSLEW
FYTDVKTRFK RFGSAKVLKT LYRKHLAEHR ALSELTEGSA YEESVCNEGS ICGSDSTFYR
QSEEHSMAET LTVALRVAEE AIDEAIDEAE FDTASQEKQD EAQYLREHRG ELVEELAKTI
VQKIISRRKT LTEMTAKYDQ DWPLEQNTDP HHHPHHQSIC DQPSCFIKHR PGLWRSHSAF
SLLSNDHPGL VQDSLQALMK EGSGSMSAWK SVDRLDNAGV SSVLKSPDGN WIALQSVQLS
RPSLLTKRKS LVYSALERES GVVSAYEGMG SDNETKTEPD SSWGAALQEI HRKMTDSNSN
LHDTRDRIPS PLMGRRGSGE EPFSDSEGNW KMKKPLLALF KRKVPAEIRR PSASQRTSII
DVNFNDFNKK DNQAHPTPDA VTSDTLTCGA TTPEPFDLES DTTGLGANQM DEELTFKLQL
LTGRVSESST GEEELDKDIV EDCDDDGPME DRDEEDESLW KMEIDLDEGR MEEENVEDDL
EVDEEMKYRL YRLVTQSRLA YFSSTDDELD KVGQSEGEWD EDNNEQEEEK TEGLTYKLCQ
LEKEVRASQF SSTEDELDRV GVDEKKTEEG EEDGSIEELA RKVCRLANQV NATQFSSTED
ELDRTGRGRD GEQGMDEEPL WKLQAEKALQ AAQLRDLASL VSASQFSSTE DELDRGEKHE
GEREQEENEG EIKSSFEIEE EWGGAVERKE SLGDLDVKMF DLRDEIEETK SESGDERATA
GNVLDYLFKI DDVQEGNTEM EAPVMRDFLE ETLTEEIREE ITEHEVHIWK DKVENETQGR
REMKMKSEVE AEKTEELGAR VEQGNQLEAK WPDENEEEAF EESKEGQGKW EATADSEEEE
AEFERIISSM LTMTLEDMQV ETLNDAAAEI GRINEEPEDM KREGSINKTR RESGFTEKMV
DAQSTNASEE TGGAKEFQSQ GNDVRSESAG RENVTELIGG DTSGKKESGE TAIRNRKEQE
ERERDPQERR TLALETNEPQ QTCRRIKVDD EEQEDARGKM ATEERVLETQ GAAADGERDR
KERDENSEED TSSLHEGLLS PEEIQHRYSA VSLRSITTEV LKVLNATEEL LQGFKGDAPL
SSTSTSLPLN TDPKKLDQQF SRLEENVYVA AGSVYSLEAE LGDLEECARG ICSSTSNMEL
SFLEEQVASA AAKVQQSELQ ICDISARIAA LKSAGLNVDT QSRFTRTKTI PVMPVTLDST
RQLRRRLPAP PVKGKEIHYF LKSVLYVANI NACSFYSFLR RQRHLNHKPR TSNTQCLDPV
TLQPAGQSYT MPVEKHVALI SPDTKHTSIN MRH
//
