Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q91V27 (MELPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Melanophilin
Alternative name(s):
Exophilin-3
Leaden protein
Slp homolog lacking C2 domains a
Short name=SlaC2-a
Synaptotagmin-like protein 2a
Gene names
Name:Mlph
Synonyms:Ln, Slac2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. Ref.2 Ref.4

Subunit structure

Binds RAB27A that has been activated by GTP-binding via its N-terminus. Binds MYO5A via its C-terminal coiled coil domain. Ref.5 Ref.6

Subcellular location

Melanosome.

Tissue specificity

Highly expressed in embryos at day 7; not detectable at day 11. Highly expressed in adult stomach; detected at lower levels in kidney, lung, skin and small intestine. Detected in melanocytes. Ref.2

Sequence similarities

Contains 1 FYVE-type zinc finger.

Contains 1 RabBD (Rab-binding) domain.

Ontologies

Keywords
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmelanocyte differentiation

Inferred from mutant phenotype Ref.2PubMed 2379821. Source: MGI

melanosome localization

Inferred from mutant phenotype PubMed 11886590Ref.4PubMed 14730011. Source: MGI

pigmentation

Inferred from mutant phenotype PubMed 17247639PubMed 2379821. Source: MGI

protein targeting

Inferred from mutant phenotype PubMed 11886590Ref.4. Source: MGI

   Cellular_componentactin cytoskeleton

Inferred from direct assay PubMed 12221080. Source: MGI

cortical actin cytoskeleton

Inferred from direct assay PubMed 16247022. Source: MGI

melanosome

Inferred from direct assay Ref.4PubMed 14730011PubMed 16137617PubMed 16247022. Source: MGI

microtubule organizing center

Inferred from direct assay PubMed 16247022. Source: MGI

stress fiber

Inferred from direct assay PubMed 16247022. Source: MGI

   Molecular_functionRab GTPase binding

Inferred from direct assay PubMed 11856727. Source: MGI

actin binding

Inferred from direct assay PubMed 12221080. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule plus-end binding

Inferred from physical interaction PubMed 16137617. Source: MGI

myosin V binding

Inferred from physical interaction Ref.4PubMed 14730011. Source: MGI

myosin binding

Inferred from direct assay PubMed 11856727. Source: MGI

protein binding

Inferred from physical interaction PubMed 11773082Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590Melanophilin
PRO_0000190223

Regions

Domain4 – 124121RabBD
Zinc finger64 – 10744FYVE-type
Coiled coil339 – 485147 Potential

Experimental info

Sequence conflict1921R → Q in BAE28452. Ref.3
Sequence conflict2541R → H in BAB41087. Ref.1
Sequence conflict3331R → W in BAE28452. Ref.3
Sequence conflict3601T → R in BAE28452. Ref.3
Sequence conflict4751E → Q in BAB41087. Ref.1
Sequence conflict4991G → S in BAE28452. Ref.3

Secondary structure

......................... 590
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q91V27 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C91444B16B8EFA1D

FASTA59065,052
        10         20         30         40         50         60 
MGKRLDLSTL TDEEAEHVWA VVQRDFDLRR REEERLQGLK GKIQKESSKR ELLSDTAHLN 

        70         80         90        100        110        120 
ETHCARCLQP YRLLLNSRRQ CLECSLFVCK SCSHAHPEEQ GWLCDPCHLA RVVKIGSLEW 

       130        140        150        160        170        180 
YYQHVRARFK RFGSAKVIRS LCGRLQGGGG SEPSLEEGNG DSEQTDEDGD LDTEARDQPL 

       190        200        210        220        230        240 
NSKKKKRLLS FRDVDFEEDS DHLVQPCSQT LGLSSVPESA HSLQSLSGEP YSEDTTSLEP 

       250        260        270        280        290        300 
EGLEETGARA LGCRPSPEVQ PCSPLPSGED AHAELDSPAA SCKSAFGTTA MPGTDDVRGK 

       310        320        330        340        350        360 
HLPSQYLADV DTSDEDSIQG PRAASQHSKR RARTVPETQI LELNKRMSAV EHLLVHLENT 

       370        380        390        400        410        420 
VLPPSAQEPT VETHPSADTE EETLRRRLEE LTSNISGSST SSEDETKPDG TFLGGSPKVC 

       430        440        450        460        470        480 
TDTGHMETQE RNPRSPGNPA RPTKSTDEEL SEMEDRVAMT ASEVQQAESE ISDIESRIAA 

       490        500        510        520        530        540 
LRAAGLTVKP SGKPRRKSGI PIFLPRVTEK LDRIPKTPPA DPDDQAKMPK ATTAVPSLLR 

       550        560        570        580        590 
RKYSPSSQGV DSGSFDRKSV YRGSLTQRNP NGRRGTARHI FAKPVMAQQP 

« Hide

References

« Hide 'large scale' references
[1]"Novel splicing isoforms of synaptotagmin-like proteins 2 and 3: identification of the Slp homology domain."
Fukuda M., Saegusa C., Mikoshiba K.
Biochem. Biophys. Res. Commun. 283:513-519(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Brain.
[2]"Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice."
Matesic L.E., Yip R., Reuss A.E., Swing D.A., O'Sullivan T.N., Fletcher C.F., Copeland N.G., Jenkins N.A.
Proc. Natl. Acad. Sci. U.S.A. 98:10238-10243(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]"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. expand/collapse author list , 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: Melanoma.
[4]"Identification of an organelle receptor for myosin-Va."
Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E., Copeland N.G., Jenkins N.A., Hammer J.A. III
Nat. Cell Biol. 4:271-278(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB27A AND MYO5A, FUNCTION.
[5]"Structural basis for the exclusive specificity of Slac2-a/melanophilin for the Rab27 GTPases."
Kukimoto-Niino M., Sakamoto A., Kanno E., Hanawa-Suetsugu K., Terada T., Shirouzu M., Fukuda M., Yokoyama S.
Structure 16:1478-1490(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-146 IN COMPLEX WITH RAB27B, SUBUNIT.
[6]"Structural basis of cargo recognitions for class V myosins."
Wei Z., Liu X., Yu C., Zhang M.
Proc. Natl. Acad. Sci. U.S.A. 110:11314-11319(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 170-208 IN COMPLEX WITH MYO5A, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB057759 mRNA. Translation: BAB41087.1.
AF384098 mRNA. Translation: AAK97435.1.
AK148274 mRNA. Translation: BAE28452.1.
CCDSCCDS15155.1.
RefSeqNP_443748.2. NM_053015.3.
UniGeneMm.105208.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZETX-ray3.00C/D1-146[»]
4KP3X-ray2.40E/F170-208[»]
4LX2X-ray1.50B176-201[»]
DisProtDP00541.
ProteinModelPortalQ91V27.
SMRQ91V27. Positions 4-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid228608. 1 interaction.
DIPDIP-31495N.
IntActQ91V27. 1 interaction.

PTM databases

PhosphoSiteQ91V27.

Proteomic databases

PaxDbQ91V27.
PRIDEQ91V27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027528; ENSMUSP00000027528; ENSMUSG00000026303.
GeneID171531.
KEGGmmu:171531.
UCSCuc007bzm.2. mouse.

Organism-specific databases

CTD79083.
MGIMGI:2176380. Mlph.

Phylogenomic databases

eggNOGNOG135976.
GeneTreeENSGT00390000013933.
HOGENOMHOG000089970.
HOVERGENHBG052454.
InParanoidQ91V27.
OrthoDBEOG76HQ10.
PhylomeDBQ91V27.
TreeFamTF331599.

Gene expression databases

ArrayExpressQ91V27.
BgeeQ91V27.
CleanExMM_MLPH.
GenevestigatorQ91V27.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR006788. Myrip/Melanophilin.
IPR010911. Znf_FYVE-typ.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF02318. FYVE_2. 1 hit.
PF04698. Rab_eff_C. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS50916. RABBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMLPH. mouse.
EvolutionaryTraceQ91V27.
NextBio371036.
PROQ91V27.
SOURCESearch...

Entry information

Entry nameMELPH_MOUSE
AccessionPrimary (citable) accession number: Q91V27
Secondary accession number(s): Q3UFV7, Q99N53
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot