MYRIP_DANRE
ID MYRIP_DANRE Reviewed; 838 AA.
AC A8T6P4;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Rab effector MyRIP;
DE AltName: Full=Exophilin-8;
DE AltName: Full=Myosin VIIa- and Rab-interacting protein;
DE AltName: Full=Synaptotagmin-like protein lacking C2 domains C;
DE Short=SlaC2-c;
DE Short=Slp homolog lacking C2 domains c;
GN Name=myrip; Synonyms=akap2; ORFNames=si:dkey-12l12.1, si:dkey-189e1.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PRKAR2AA.
RC TISSUE=Embryo;
RX PubMed=17827149; DOI=10.1074/jbc.m705167200;
RA Goehring A.S., Pedroja B.S., Hinke S.A., Langeberg L.K., Scott J.D.;
RT "MyRIP anchors protein kinase A to the exocyst complex.";
RL J. Biol. Chem. 282:33155-33167(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: May link secretory vesicles to actin filaments (By
CC similarity). May function as a protein kinase A-anchoring protein
CC (AKAP). May act as a scaffolding protein that links PKA to components
CC of the exocytosis machinery, thus facilitating exocytosis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with prkar2aa. {ECO:0000269|PubMed:17827149}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}.
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DR EMBL; EF694835; ABV53439.1; -; mRNA.
DR EMBL; BX005057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A8T6P4; -.
DR SMR; A8T6P4; -.
DR STRING; 7955.ENSDARP00000099429; -.
DR PaxDb; A8T6P4; -.
DR PRIDE; A8T6P4; -.
DR ZFIN; ZDB-GENE-080123-1; myripb.
DR eggNOG; ENOG502QPUS; Eukaryota.
DR HOGENOM; CLU_008568_0_0_1; -.
DR InParanoid; A8T6P4; -.
DR OMA; LNAMMMR; -.
DR PhylomeDB; A8T6P4; -.
DR ChiTaRS; si:dkey-12l12.1; zebrafish.
DR PRO; PR:A8T6P4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
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; -; 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 Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF04698; Rab_eff_C; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..838
FT /note="Rab effector MyRIP"
FT /id="PRO_0000417354"
FT DOMAIN 4..124
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT ZN_FING 58..112
FT /note="FYVE-type"
FT REGION 263..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 188..237
FT /evidence="ECO:0000255"
FT COILED 714..833
FT /evidence="ECO:0000255"
FT COMPBIAS 263..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 96250 MW; 32C36042B6A8BAB3 CRC64;
MGRKLDLSGL SNNEAEHVLR VVQRDMQLRK KEEERLSEMK QELEEEGSRC LLLSKQQKFN
EHCCIRCCSP FTFLLNPKRQ CLDCHYNICK SCCSYSQSER GYICAACQKS RHLRTQSLEW
FYNNVKSRFK RFGSAKVLKT LYRKHIIERG ALSELPEVSA HEGSNDNGSI CDGSDSTLYK
QSEGHSMADT LTVALRVAEE AIEEAIAKAE NYKDSLEKQN EARYLHEHKE ELIEELATTI
VQKIIQRGKR PEIQEEYEFV WPQNQKSELP SPTSTQNPLA TQNSHSTSQP GAVAQSDISK
RSRSAYSSDD SPEKGPEVGM APGVPKSTEV ETDIQNYSSL RRESRALSLP GWKSVDRLEN
SSASSVLQSP DGNWIALQSS QHSRPSLLTK RKSLVFSVLE KESGVVSAYD EMGSDSDPED
QGGWGAALLQ FRRRLSDETY YTDSQHDPEW TFTQHPPITS PSSGQYTNTE TLNSDSETSP
SPSTRARRAP VMKKGPPETH LYPYYRHPAD IVALPQLKPD VLDVNFNPHL GGDSSDGEER
SEQVKRSRRR RKSKRETSEH SRAHNALYSA ATAENSTVLL NAMMMRRQQS QENTVPLNHQ
TPDSVTSPDI LTFNNMSPEP EYQNTLAHNS SAASLPLLSQ LGSNNPGFAP QDPLLRAFPV
NETLEEELKY KLSELIGQVS ERDVKSSDFE PISEVGNKQE DRVSEKDSGK LRPKERRESK
RESKLREMEK QSERQTVKLM DTSDAVRQIN IERQMKKERE RQRDIERQVE RERERQRELE
KQIEKDRERR REIEMQVEKK QERQKEMEKQ LKQEQERQSE IERDLEKKRK SIRMEKRN
