位置:首页 > 蛋白库 > MYRIP_MOUSE
MYRIP_MOUSE
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   03-AUG-2022, entry version 149.
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}.
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; 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; Q8K3I4; -.
DR   PRIDE; Q8K3I4; -.
DR   ProteomicsDB; 293609; -.
DR   Antibodypedia; 28983; 175 antibodies from 27 providers.
DR   DNASU; 245049; -.
DR   Ensembl; ENSMUST00000048121; ENSMUSP00000046891; ENSMUSG00000041794.
DR   GeneID; 245049; -.
DR   KEGG; mmu:245049; -.
DR   UCSC; uc009scn.1; mouse.
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; DNGQCIQ; -.
DR   OrthoDB; 492485at2759; -.
DR   PhylomeDB; Q8K3I4; -.
DR   TreeFam; TF331599; -.
DR   BioGRID-ORCS; 245049; 0 hits in 72 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 152 other 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:0030667; C:secretory granule membrane; ISO:MGI.
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; -; 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   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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024