MYRIP_RAT
ID MYRIP_RAT Reviewed; 856 AA.
AC Q7TNY7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Retina;
RA Ramalho J.S., Futter C., Seabra M.;
RT "Myrip (Slac2-c) interacting with Myo7a/Rab27a plays a role in melanosome
RT transport in retinal pigmented epithelium.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INTERACTION WITH EXOC3 AND EXOC4, AND SUBCELLULAR LOCATION.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). Functions as a protein kinase A-anchoring protein (AKAP).
CC May act as a scaffolding protein that links PKA to components of the
CC exocytosis machinery, thus facilitating exocytosis, including insulin
CC release. {ECO:0000250, ECO:0000269|PubMed:17827149}.
CC -!- SUBUNIT: Binds MYO5A, MYO7A and F-actin. Binds RAB27A that has been
CC activated by GTP-binding via its N-terminus (By similarity). Interacts
CC with PRKAR2A. Interacts with components of the exocyst complex,
CC including EXOC3 and EXOC4. {ECO:0000250, ECO:0000269|PubMed:17827149}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:17827149}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:17827149}.
CC Melanosome {ECO:0000250|UniProtKB:Q8K3I4}. Note=In presynaptic and
CC postsynaptic areas in photoreceptor cells and in the basal microvilli
CC of retinal pigment epithelium cells. Associated with melanosomes.
CC Colocalizes with actin filaments. {ECO:0000250|UniProtKB:Q8K3I4}.
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DR EMBL; AY331984; AAP94626.1; -; mRNA.
DR RefSeq; NP_878264.1; NM_182844.1.
DR AlphaFoldDB; Q7TNY7; -.
DR SMR; Q7TNY7; -.
DR STRING; 10116.ENSRNOP00000025460; -.
DR iPTMnet; Q7TNY7; -.
DR PhosphoSitePlus; Q7TNY7; -.
DR PaxDb; Q7TNY7; -.
DR PRIDE; Q7TNY7; -.
DR GeneID; 360034; -.
DR KEGG; rno:360034; -.
DR UCSC; RGD:727731; rat.
DR CTD; 25924; -.
DR RGD; 727731; Myrip.
DR eggNOG; ENOG502QPUS; Eukaryota.
DR InParanoid; Q7TNY7; -.
DR PhylomeDB; Q7TNY7; -.
DR PRO; PR:Q7TNY7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; IDA:UniProtKB.
DR GO; GO:0000145; C:exocyst; ISO:RGD.
DR GO; GO:0042470; C:melanosome; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB.
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_0000281024"
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 /evidence="ECO:0000250"
FT REGION 193..209
FT /note="PKA-binding"
FT /evidence="ECO:0000250"
FT REGION 232..248
FT /note="Negative regulation of PKA-binding"
FT /evidence="ECO:0000250"
FT REGION 251..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..856
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 592..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..463
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 547..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 MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3I4"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 856 AA; 94985 MW; 501FEE28739E938B CRC64;
MGRKLDLSGL TDDETEHVLQ VVQRDFNLRK KEEDRLSEMK QRLAEENSKC SILSKHQKFV
ERCCMRCCSP FTFLVNARRR CGECKFSVCK SCCSYQKHEK LWVCCVCQQA RLLRTQSLEW
FYNNVKTRFK RFGSAKVLKN LYKKHRLESG ACFDILGGGL YEPNLENEGS ISGSDSTFYR
QSEGHSMMDT LAVALQVAEE AIEEAISKAE SQRDSLDKQN EASYLRDHRQ ELAEELAGTI
LQRIIRKQKD KADLHAEEEE PECTRPQSSG VKARGEGTAA PPGRHKARAA LWRSQSAFSF
TTEDTLKTSS AEAAPRQPKD RAQRLLEESA LPSWRSMDGL DGKNLVPLLQ SPDGNWMTLK
DSSRQPPTRL LAKPKSRTFQ ALEVASSVAS AYDELGSDSE EDFDYSEALS KLRPPSQGRL
KQPQPQPAQA QSSGQGPLAT SPSNPEAMCS DSETSSTSSS REAGCRAKLL WLQRKAPKNP
SAEKTHLQGE LDVNFNPQAA GGETSDSSDP EETLHTADRR ARRWRRARVG PEESNRGLPS
PSAYPPALHT AQVSDNVSET DISNEAQNSR SSTDSAEEKL RNRLYELAMK MSEKETSSGE
DQESESKTEP KNQKGSLSSE ENNQGVQEEL KKKCSAVSLC NISTEVLKVI NATEELIAES
AGPWEIPPVS TDRDNGMFPL GTDQRSLDKQ LTSLEENVYL AAGTVYGLEG QLSELEDAAR
CIHSSTGETE LADLEDQVAA AAAQVHHAEL QISDIESRIS ALTIAGLNIA PCVRLTRRRD
QKQRSQVQTI DTSRQQRRKL PAPPVKAEKI EASSVTPIKT FNRNFLLQGS STNRPTASTS
NTKDLMEPVL ESAVMY
