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Protein

Rab effector MyRIP

Gene

Myrip

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri63 – 10543FYVE-typeAdd
BLAST

GO - Molecular functioni

  • actin binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • myosin binding Source: MGI
  • protein kinase A binding Source: UniProtKB
  • Rab GTPase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Rab effector MyRIP
Alternative name(s):
Exophilin-8
Myosin-VIIa- and Rab-interacting protein
Synaptotagmin-like protein lacking C2 domains C
Short name:
SlaC2-c
Short name:
Slp homolog lacking C2 domains c
Gene namesi
Name:Myrip
Synonyms:Slac2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2384407. Myrip.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • apical plasma membrane Source: Ensembl
  • dense core granule Source: UniProtKB
  • exocyst Source: UniProtKB
  • melanosome Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • photoreceptor outer segment Source: UniProtKB
  • secretory granule membrane Source: Ensembl
  • synapse Source: UniProtKB
  • transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi197 – 1971V → P: Loss of PRKAR2A-binding; when associated with P-206. 1 Publication
Mutagenesisi206 – 2061I → P: Loss of PRKAR2A-binding; when associated with P-197. 1 Publication
Mutagenesisi236 – 2361L → P: Increased PRKAR2A-binding; when associated with P-245.
Mutagenesisi245 – 2451I → P: Increased PRKAR2A-binding; when associated with P-245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 856856Rab effector MyRIPPRO_0000190225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei351 – 3511PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8K3I4.
PaxDbiQ8K3I4.
PRIDEiQ8K3I4.

PTM databases

iPTMnetiQ8K3I4.
PhosphoSiteiQ8K3I4.

Expressioni

Tissue specificityi

Detected in brain, skin, heart, lung, adrenal medulla, pancreas, intestine, liver, kidney, skeletal muscle and testis. Detected in cochlear and vestibular hair cells in the inner ear, and in photoreceptor and pigment epithelium cells in the retina.2 Publications

Gene expression databases

BgeeiQ8K3I4.
CleanExiMM_MYRIP.
ExpressionAtlasiQ8K3I4. baseline and differential.
GenevisibleiQ8K3I4. MM.

Interactioni

Subunit structurei

Binds RAB27A that has been activated by GTP-binding via its N-terminus. Binds MYO5A, MYO7A and F-actin. Interacts with PRKAR2A. Interacts with components of the exocyst complex, including EXOC3 and EXOC4.2 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • myosin binding Source: MGI
  • protein kinase A binding Source: UniProtKB
  • Rab GTPase binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046891.

Structurei

3D structure databases

ProteinModelPortaliQ8K3I4.
SMRiQ8K3I4. Positions 4-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 124121RabBDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni143 – 560418Myosin-bindingAdd
BLAST
Regioni193 – 20917PRKAR2A-bindingAdd
BLAST
Regioni232 – 24817Negative regulation of PRKAR2A-bindingAdd
BLAST
Regioni495 – 856362Actin-bindingAdd
BLAST

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.Curated
Contains 1 RabBD (Rab-binding) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri63 – 10543FYVE-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IHBX. Eukaryota.
ENOG41126RD. LUCA.
GeneTreeiENSGT00390000013933.
HOGENOMiHOG000113712.
HOVERGENiHBG052562.
InParanoidiQ8K3I4.
OMAiARCIHSG.
OrthoDBiEOG76HQ10.
PhylomeDBiQ8K3I4.
TreeFamiTF331599.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR006788. Myrip/Melanophilin.
IPR010911. Rab_BD.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02318. FYVE_2. 1 hit.
PF04698. Rab_eff_C. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50916. RABBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K3I4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRKLDLSGL TDDETEHVLQ VVQRDFNLRK KEEDRLSEMK QRLAEENSKC
60 70 80 90 100
SILSKHQKFV ERCCMRCCSP FTFLVNARRR CGECKFSVCK SCCSYQKHEK
110 120 130 140 150
LWVCCVCQQA RLLRTQSLEW FYNNVKSRFK RFGSAKVLKN LYRKHRLESG
160 170 180 190 200
ACFDILGGGL FEPNLENEGS ISGSDSTFYR QSEGHSMMDT LAVALRVAEE
210 220 230 240 250
AIEEAISKAE SHGDSLDKQN EASYLRDHKQ ELTEELAGTI LQRIIRKQKD
260 270 280 290 300
KAELRAEEEE PEWPRSQSGS VKARGEGTTA PPGRHKARAT FRRSQSAFSF
310 320 330 340 350
TMEDALKSGS AEAAPRSPKD RAQRLLEEAA LPSWRSMDGL DGTNLAPLLQ
360 370 380 390 400
SPDGNWMTLK DGSRQPPTRL LTKPKSGTFQ ALEVASSVTS AYDEIGSDSE
410 420 430 440 450
EDFDYSEALS KLCPPSQSRL KQPQPQPTQA QSSGQGPLAT SPSNPEAMCS
460 470 480 490 500
DSETSSTSSS REAGCRAKLS WLQRKAPKNP AVEKMPLQGE LDVNFNPQAA
510 520 530 540 550
GGETSDSSDP EETLRTAERR ARRWRRARVG PEESNRGLPS PGAHPRALHT
560 570 580 590 600
AQVSDNVSET DISNETQNSR SSTDSVEEKL RNRLYELAMK MSEKETSSGE
610 620 630 640 650
DQESESKAEP KNQKGSLSSE ENNQGVQEEL KKKCSAVSLC NISTEVLKVI
660 670 680 690 700
NATEELIAES AGPWEIPPVS TDRENGMFPL GTDQVRLDKQ LTSLEENVYL
710 720 730 740 750
AAGTVYGLEG QLSELEDAAR CIHSSTGETE LADLEDQVAA AAAQVHHAEL
760 770 780 790 800
QISDIESRIS ALTIAGLNIA PCVRLTRRRD QKQRSQVQTI DTSRQQRRKL
810 820 830 840 850
PAPPVKAEKI EASSVTPIKT FNRNFLLQGS STNRPTASTG DTKDLMEPDL

ESAVMY
Length:856
Mass (Da):94,924
Last modified:October 1, 2002 - v1
Checksum:i1150ABB83B102C8A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661S → P in AAI29853 (PubMed:15489334).Curated
Sequence conflicti322 – 3221A → T in AAI29853 (PubMed:15489334).Curated
Sequence conflicti400 – 4001E → G in AAM43955 (PubMed:11964381).Curated
Sequence conflicti408 – 4081A → R in BAC15554 (PubMed:12062444).Curated
Sequence conflicti409 – 4091L → F in AAM43955 (PubMed:11964381).Curated
Sequence conflicti593 – 5931E → K in AAM43955 (PubMed:11964381).Curated
Sequence conflicti593 – 5931E → K in AAI29852 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF396688 mRNA. Translation: AAM43955.1.
AY099470 mRNA. Translation: AAM44403.1.
AB083782 mRNA. Translation: BAC15554.1.
AK038988 mRNA. Translation: BAC30194.1.
AK083225 mRNA. Translation: BAC38816.1.
BC129851 mRNA. Translation: AAI29852.1.
BC129852 mRNA. Translation: AAI29853.1.
CCDSiCCDS23627.1.
RefSeqiNP_653140.1. NM_144557.5.
XP_006512188.1. XM_006512125.2.
UniGeneiMm.100936.

Genome annotation databases

EnsembliENSMUST00000048121; ENSMUSP00000046891; ENSMUSG00000041794.
GeneIDi245049.
KEGGimmu:245049.
UCSCiuc009scn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF396688 mRNA. Translation: AAM43955.1.
AY099470 mRNA. Translation: AAM44403.1.
AB083782 mRNA. Translation: BAC15554.1.
AK038988 mRNA. Translation: BAC30194.1.
AK083225 mRNA. Translation: BAC38816.1.
BC129851 mRNA. Translation: AAI29852.1.
BC129852 mRNA. Translation: AAI29853.1.
CCDSiCCDS23627.1.
RefSeqiNP_653140.1. NM_144557.5.
XP_006512188.1. XM_006512125.2.
UniGeneiMm.100936.

3D structure databases

ProteinModelPortaliQ8K3I4.
SMRiQ8K3I4. Positions 4-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046891.

PTM databases

iPTMnetiQ8K3I4.
PhosphoSiteiQ8K3I4.

Proteomic databases

MaxQBiQ8K3I4.
PaxDbiQ8K3I4.
PRIDEiQ8K3I4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048121; ENSMUSP00000046891; ENSMUSG00000041794.
GeneIDi245049.
KEGGimmu:245049.
UCSCiuc009scn.1. mouse.

Organism-specific databases

CTDi25924.
MGIiMGI:2384407. Myrip.

Phylogenomic databases

eggNOGiENOG410IHBX. Eukaryota.
ENOG41126RD. LUCA.
GeneTreeiENSGT00390000013933.
HOGENOMiHOG000113712.
HOVERGENiHBG052562.
InParanoidiQ8K3I4.
OMAiARCIHSG.
OrthoDBiEOG76HQ10.
PhylomeDBiQ8K3I4.
TreeFamiTF331599.

Miscellaneous databases

PROiQ8K3I4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K3I4.
CleanExiMM_MYRIP.
ExpressionAtlasiQ8K3I4. baseline and differential.
GenevisibleiQ8K3I4. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR006788. Myrip/Melanophilin.
IPR010911. Rab_BD.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02318. FYVE_2. 1 hit.
PF04698. Rab_eff_C. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50916. RABBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes."
    El-Amraoui A., Schonn J.-S., Kuessel-Andermann P., Blanchard S., Desnos C., Henry J.-P., Wolfrum U., Darchen F., Petit C.
    EMBO Rep. 3:463-470(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Inner ear.
  2. "Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions."
    Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T., Izumi T.
    FEBS Lett. 517:233-238(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin."
    Fukuda M., Kuroda T.S.
    J. Biol. Chem. 277:43096-43103(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RAB27A; MYO5A; MYO7A AND F-ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus and Hypothalamus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: FUNCTION, INTERACTION WITH PRKAR2A; EXOC3 AND EXOC4, MUTAGENESIS OF VAL-197 AND ILE-206.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Lung and Pancreas.

Entry informationi

Entry nameiMYRIP_MOUSE
AccessioniPrimary (citable) accession number: Q8K3I4
Secondary accession number(s): A1L320
, A1L321, Q8CFC0, Q8K4H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.