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Database: UniProt
Entry: I3MYW6_ICTTR
LinkDB: I3MYW6_ICTTR
Original site: I3MYW6_ICTTR 
ID   I3MYW6_ICTTR            Unreviewed;       982 AA.
AC   I3MYW6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Junction mediating and regulatory protein, p53 cofactor {ECO:0000313|Ensembl:ENSSTOP00000017312.2};
GN   Name=JMY {ECO:0000313|Ensembl:ENSSTOP00000017312.2};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000017312.2, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000017312.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR   EMBL; AGTP01055343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01055344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3MYW6; -.
DR   STRING; 43179.ENSSTOP00000017312; -.
DR   Ensembl; ENSSTOT00000024495.2; ENSSTOP00000017312.2; ENSSTOG00000021490.2.
DR   eggNOG; ENOG502QRHU; Eukaryota.
DR   GeneTree; ENSGT00510000046704; -.
DR   HOGENOM; CLU_012316_2_0_1; -.
DR   InParanoid; I3MYW6; -.
DR   TreeFam; TF331023; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:Ensembl.
DR   GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR   InterPro; IPR031738; JMY/WHAMM.
DR   InterPro; IPR031808; JMY/WHAMM_N.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR23330:SF8; JUNCTION-MEDIATING AND -REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR23330; P300 TRANSCRIPTIONAL COFACTOR JMY-RELATED; 1.
DR   Pfam; PF15871; JMY; 1.
DR   Pfam; PF15920; WHAMM-JMY_N; 2.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51082; WH2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT   DOMAIN          915..932
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          50..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          961..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          319..346
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          576..610
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        50..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..822
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..982
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   982 AA;  110771 MW;  46D8AC4B86A18B5B CRC64;
     MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE
     QAGTPVSDGT RGPGSPVGKG RPEATGSATP VRSPGSRRSP TWAEGGSPRS ARCLRGDPPQ
     RSPAGRGAES LLRSPARAKP SPVRKGVEAR DAAGSATATQ TAPKEAPVSS VRVVSASGAV
     SEEIEVLEMV REDETPLALS DAEQPPPAAE PESPAEECSW AGLFSFQDLR AVHQQLCSVN
     SQLEPCLPVF PEEPSGMWTV LFGGAPEMTE QEIDTLCYQL QVYLGHGLDT CGWKILSQVL
     FTETDDPEEY YESLSELRQK GYEEVLQRAR KRIQELLDKH KNTESMVELL DLYQMEDEAY
     SSLAEATTEL YQYLLQPFRD MRELAMLRRQ QIKISMENDY LGPRRIESLQ KEDADWQRKA
     HMAVLSIQDL TVKYFEITAK AQKAVYDRMR ADQKKFGKAS WAAAAERMEK LQYAVSKETL
     QMMRAKEICL EQRKHALKEE MQSLQGGTEA IARLDQLEAD YYDLQLQLYE VQFEILKCEE
     LLLTAQLESI KRLISEKRDE VVYYDTYESM EAMLEKEEMA ASVHAQREEL QKLQQKARQL
     EARRGRVSAK KAYLRNKKEI CIAKHNEKFQ QRIQSEEEYR THHMVQLKRE KVHDEEERKS
     AWVSQERQRT LDRLRTFKQR YPGQVILKST RLRLAHARRK SATSPVPHED PCDSLPGVLQ
     VEGKTEEVGE GRGQLGSSQT TESQHLSQLE DNSLAQLEAT SLPLSGVTSE LPPTASLPLL
     NSSDLEPCSV STDPFPPPLP PTPPPPPPPP PPPPPPPLPV AKDNTANPET LEKGLPRKEG
     NEKRIPKSAS APSAHLFDSS QLVSARKKLR KTAEGLQRRR VSSPMDEVLA SLKRGSFHLK
     KVEQRTLPPF PDEDDSNNIL AQIRKGVKLK KVQKEVLRES FTLLPDTDPL TRSIHEALRR
     IKEASPESED EEEALPCTDW EN
//
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