ID A0A1S3F3Q1_DIPOR Unreviewed; 998 AA.
AC A0A1S3F3Q1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Junction-mediating and -regulatory protein {ECO:0000313|RefSeq:XP_012871263.1};
GN Name=Jmy {ECO:0000313|RefSeq:XP_012871263.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012871263.1};
RN [1] {ECO:0000313|RefSeq:XP_012871263.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012871263.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR RefSeq; XP_012871263.1; XM_013015809.1.
DR AlphaFoldDB; A0A1S3F3Q1; -.
DR STRING; 10020.ENSDORP00000005168; -.
DR GeneID; 105985305; -.
DR KEGG; dord:105985305; -.
DR CTD; 133746; -.
DR InParanoid; A0A1S3F3Q1; -.
DR OrthoDB; 5354952at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
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:UP000081671}.
FT DOMAIN 931..948
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 50..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 332..359
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 589..623
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 804..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..998
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 112146 MW; DD54A5E851FDAFDB CRC64;
MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE
QAGARGGAEP GAPASDGTRG PGSPAGKCRP EAGASATPVR SPGPRRSPIW ADGGSPRSPR
SLRGDPLLRG PAGKGAESPL RSPARAKPSP VRKGAEPRDA TRPATAASPP APREAPVSSV
RVVSASGAVS EEIEVLEMVR EDETPLTVTD AEQPPPAAAT TTEPESPAEE CSWAGLFSFQ
DLRAVHQQLC SVNSQLEPCL PVFPEEPSGM WTVLFGGAPE MSEQEIDALC YQLQVYLGHG
LDTCGWKILS QVLFTETDDP EEYYESLSEL RQKGYEEVLQ RARKRIQELL DKHKNIESMV
ELLDLYQMED EAYSSLAEAT TELYQYLLQP FRDMRELAML RRQQIKISME NDYLGPRRIE
SLQKEDADWQ RKAHMAVLSI QDLTVKYFEI TAKAQKAVYD RMRADQKKFG KASWAAAAER
MEKLQYAVSK ETLQMMRAKE ICLEQRKHAL KEEMQSLQGG TEAIAQLDQL EADYYDLQLQ
LYEVQFEILK CEELLLTAQL ESIKRLISEK RDEVVYYDTY ESMEAMLEKE EMAASVHAQR
EELQKLQQKA RQLEARRGRV SAKKAYLRNK KEICISKHNE KFQQRFRSEE EYRNHHTAQL
KKEKLLDEEE RKSAWVSQER QRTLDRLRTF KQRYPGQVIL KSTRLRLAHA RRKSAASPMS
QEDQGDSLPG VLQGMEKAEE LGERRDPLGS PQTTEPQSLA QLEDSSLAQL EATSLPLSGV
VSELPPTASL PLLTSNDLEP CSGTIDPVPP PLPPTPLPPP PPPPPPPPPP PLPVAKDECA
DVTAETLEKG LPRKEGTEKR IPKSASAPSA HLFDSSQLVS ARKKLRKTAE SLQRRRVSSP
MDEVLASLKR GSFHLKKVEQ RTLPPFPDED DSNNILAQIR KGVKLKKVQK DVLRESFTLL
PDTDPLTRSI HEALRRIKEA SPESEDEEEA LPSTDWEN
//