ID MYRIP_MOUSE Reviewed; 856 AA.
AC Q8K3I4; A1L320; A1L321; Q8CFC0; Q8K4H5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 157.
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=Slac2c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Inner ear;
RX PubMed=11964381; DOI=10.1093/embo-reports/kvf090;
RA El-Amraoui A., Schonn J.-S., Kuessel-Andermann P., Blanchard S., Desnos C.,
RA Henry J.-P., Wolfrum U., Darchen F., Petit C.;
RT "MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal
RT melanosomes.";
RL EMBO Rep. 3:463-470(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=12062444; DOI=10.1016/s0014-5793(02)02634-0;
RA Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T.,
RA Izumi T.;
RT "Melanophilin directly links Rab27a and myosin Va through its distinct
RT coiled-coil regions.";
RL FEBS Lett. 517:233-238(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RAB27A; MYO5A; MYO7A AND
RP F-ACTIN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12221080; DOI=10.1074/jbc.m203862200;
RA Fukuda M., Kuroda T.S.;
RT "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a
RT novel linker protein that interacts with Rab27, myosin Va/VIIa, and
RT actin.";
RL J. Biol. Chem. 277:43096-43103(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INTERACTION WITH PRKAR2A; EXOC3 AND EXOC4, AND MUTAGENESIS OF
RP VAL-197 AND ILE-206.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Rab effector protein involved in melanosome transport. Serves
CC as link between melanosome-bound RAB27A and the motor proteins MYO5A
CC and MYO7A. May link RAB27A-containing vesicles to actin filaments.
CC Functions as a protein kinase A-anchoring protein (AKAP). May act as a
CC scaffolding protein that links PKA to components of the exocytosis
CC machinery, thus facilitating exocytosis, including insulin release.
CC {ECO:0000269|PubMed:17827149}.
CC -!- SUBUNIT: Binds RAB27A that has been activated by GTP-binding via its N-
CC terminus. Binds MYO5A, MYO7A and F-actin. Interacts with PRKAR2A.
CC Interacts with components of the exocyst complex, including EXOC3 and
CC EXOC4. {ECO:0000269|PubMed:12221080, ECO:0000269|PubMed:17827149}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12221080}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}.
CC Melanosome {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}.
CC Note=In presynaptic and postsynaptic areas in photoreceptor cells and
CC in the basal microvilli of retinal pigment epithelium cells. Associated
CC with melanosomes. Colocalizes with actin filaments. In insulin-
CC secreting cells, associated with dense core secretory granules.
CC {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}.
CC -!- TISSUE SPECIFICITY: Detected in brain, skin, heart, lung, adrenal
CC medulla, pancreas, intestine, liver, kidney, skeletal muscle and
CC testis. Detected in cochlear and vestibular hair cells in the inner
CC ear, and in photoreceptor and pigment epithelium cells in the retina.
CC {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}.
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DR EMBL; AF396688; AAM43955.1; -; mRNA.
DR EMBL; AY099470; AAM44403.1; -; mRNA.
DR EMBL; AB083782; BAC15554.1; -; mRNA.
DR EMBL; AK038988; BAC30194.1; -; mRNA.
DR EMBL; AK083225; BAC38816.1; -; mRNA.
DR EMBL; BC129851; AAI29852.1; -; mRNA.
DR EMBL; BC129852; AAI29853.1; -; mRNA.
DR CCDS; CCDS23627.1; -.
DR RefSeq; NP_653140.1; NM_144557.5.
DR RefSeq; XP_006512188.1; XM_006512125.2.
DR AlphaFoldDB; Q8K3I4; -.
DR SMR; Q8K3I4; -.
DR STRING; 10090.ENSMUSP00000046891; -.
DR iPTMnet; Q8K3I4; -.
DR PhosphoSitePlus; Q8K3I4; -.
DR MaxQB; Q8K3I4; -.
DR PaxDb; 10090-ENSMUSP00000046891; -.
DR ProteomicsDB; 293609; -.
DR Antibodypedia; 28983; 186 antibodies from 27 providers.
DR DNASU; 245049; -.
DR Ensembl; ENSMUST00000048121.13; ENSMUSP00000046891.7; ENSMUSG00000041794.14.
DR GeneID; 245049; -.
DR KEGG; mmu:245049; -.
DR UCSC; uc009scn.1; mouse.
DR AGR; MGI:2384407; -.
DR CTD; 25924; -.
DR MGI; MGI:2384407; Myrip.
DR VEuPathDB; HostDB:ENSMUSG00000041794; -.
DR eggNOG; ENOG502QPUS; Eukaryota.
DR GeneTree; ENSGT00950000183138; -.
DR HOGENOM; CLU_008568_0_0_1; -.
DR InParanoid; Q8K3I4; -.
DR OMA; NIAPCVH; -.
DR OrthoDB; 2967336at2759; -.
DR PhylomeDB; Q8K3I4; -.
DR TreeFam; TF331599; -.
DR BioGRID-ORCS; 245049; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Myrip; mouse.
DR PRO; PR:Q8K3I4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K3I4; Protein.
DR Bgee; ENSMUSG00000041794; Expressed in pigmented layer of retina and 153 other cell types or tissues.
DR ExpressionAtlas; Q8K3I4; baseline and differential.
DR Genevisible; Q8K3I4; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; ISS:UniProtKB.
DR GO; GO:0000145; C:exocyst; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IDA:MGI.
DR GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; TAS:MGI.
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; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoplasmic vesicle; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..856
FT /note="Rab effector MyRIP"
FT /id="PRO_0000190225"
FT DOMAIN 4..124
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT ZN_FING 63..105
FT /note="FYVE-type"
FT REGION 143..560
FT /note="Myosin-binding"
FT REGION 193..209
FT /note="PRKAR2A-binding"
FT REGION 232..248
FT /note="Negative regulation of PRKAR2A-binding"
FT REGION 252..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..856
FT /note="Actin-binding"
FT REGION 592..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TNY7"
FT MUTAGEN 197
FT /note="V->P: Loss of PRKAR2A-binding; when associated with
FT P-206."
FT /evidence="ECO:0000269|PubMed:17827149"
FT MUTAGEN 206
FT /note="I->P: Loss of PRKAR2A-binding; when associated with
FT P-197."
FT /evidence="ECO:0000269|PubMed:17827149"
FT MUTAGEN 236
FT /note="L->P: Increased PRKAR2A-binding; when associated
FT with P-245."
FT MUTAGEN 245
FT /note="I->P: Increased PRKAR2A-binding; when associated
FT with P-245."
FT CONFLICT 266
FT /note="S -> P (in Ref. 5; AAI29853)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="A -> T (in Ref. 5; AAI29853)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="E -> G (in Ref. 1; AAM43955)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="A -> R (in Ref. 2; BAC15554)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="L -> F (in Ref. 1; AAM43955)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> K (in Ref. 1; AAM43955 and 5; AAI29852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 856 AA; 94924 MW; 1150ABB83B102C8A CRC64;
MGRKLDLSGL TDDETEHVLQ VVQRDFNLRK KEEDRLSEMK QRLAEENSKC SILSKHQKFV
ERCCMRCCSP FTFLVNARRR CGECKFSVCK SCCSYQKHEK LWVCCVCQQA RLLRTQSLEW
FYNNVKSRFK RFGSAKVLKN LYRKHRLESG ACFDILGGGL FEPNLENEGS ISGSDSTFYR
QSEGHSMMDT LAVALRVAEE AIEEAISKAE SHGDSLDKQN EASYLRDHKQ ELTEELAGTI
LQRIIRKQKD KAELRAEEEE PEWPRSQSGS VKARGEGTTA PPGRHKARAT FRRSQSAFSF
TMEDALKSGS AEAAPRSPKD RAQRLLEEAA LPSWRSMDGL DGTNLAPLLQ SPDGNWMTLK
DGSRQPPTRL LTKPKSGTFQ ALEVASSVTS AYDEIGSDSE EDFDYSEALS KLCPPSQSRL
KQPQPQPTQA QSSGQGPLAT SPSNPEAMCS DSETSSTSSS REAGCRAKLS WLQRKAPKNP
AVEKMPLQGE LDVNFNPQAA GGETSDSSDP EETLRTAERR ARRWRRARVG PEESNRGLPS
PGAHPRALHT AQVSDNVSET DISNETQNSR SSTDSVEEKL RNRLYELAMK MSEKETSSGE
DQESESKAEP KNQKGSLSSE ENNQGVQEEL KKKCSAVSLC NISTEVLKVI NATEELIAES
AGPWEIPPVS TDRENGMFPL GTDQVRLDKQ LTSLEENVYL AAGTVYGLEG QLSELEDAAR
CIHSSTGETE LADLEDQVAA AAAQVHHAEL QISDIESRIS ALTIAGLNIA PCVRLTRRRD
QKQRSQVQTI DTSRQQRRKL PAPPVKAEKI EASSVTPIKT FNRNFLLQGS STNRPTASTG
DTKDLMEPDL ESAVMY
//
