ID MLPH_MOUSE STANDARD; PRT; 590 AA. AC Q91V27; Q99N53; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Melanophilin (Exophilin 3) (Leaden protein) (Synaptotagmin-like DE protein 2a) (Slac2-a) (Slp homologue lacking C2 domains-a). GN Name=Mlph; Synonyms=Ln, Slac2a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/c; TISSUE=Brain; RX MEDLINE=21226169; PubMed=11327731; DOI=10.1006/bbrc.2001.4803; RA Fukuda M., Saegusa C., Mikoshiba K.; RT "Novel splicing isoforms of synaptotagmin-like proteins 2 and 3: RT identification of the Slp homology domain."; RL Biochem. Biophys. Res. Commun. 283:513-519(2001). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=21417727; PubMed=11504925; DOI=10.1073/pnas.181336698; RA Matesic L.E., Yip R., Reuss A.E., Swing D.A., O'Sullivan T.N., RA Fletcher C.F., Copeland N.G., Jenkins N.A.; RT "Mutations in Mlph, encoding a member of the Rab effector family, RT cause the melanosome transport defects observed in leaden mice."; RL Proc. Natl. Acad. Sci. U.S.A. 98:10238-10243(2001). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Breast cancer; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP INTERACTION WITH RAB27A AND MYO5A, AND FUNCTION. RX MEDLINE=21941127; PubMed=11887186; DOI=10.1038/ncb760; RA Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E., RA Copeland N.G., Jenkins N.A., Hammer J.A. III; RT "Identification of an organelle receptor for myosin-Va."; RL Nat. Cell Biol. 4:271-278(2002). CC -!- FUNCTION: Rab effector protein involved in melanosome transport. CC Serves as link between melanosome-bound RAB27A and the motor CC protein MYO5A. CC -!- SUBUNIT: Binds RAB27A that has been activated by GTP-binding via CC its N-terminus. Binds MYO5A via its C-terminal coiled coil domain. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. Associates with melanosomes. CC -!- TISSUE SPECIFICITY: Highly expressed in embryos at day 7; not CC detectable at day 11. Highly expressed in adult stomach; detected CC at lower levels in kidney, lung, skin and small intestine. CC Detected in melanocytes. CC -!- SIMILARITY: Contains 1 FYVE-type zinc finger. CC -!- SIMILARITY: Contains 1 Rab-binding (RabBD) domain. 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; AB057759; BAB41087.1; -. DR EMBL; AF384098; AAK97435.1; -. DR EMBL; BC006900; AAH06900.1; -. DR IntAct; Q91V27; -. DR MGD; MGI:2176380; Mlph. DR GO; GO:0015629; C:actin cytoskeleton; IDA. DR GO; GO:0003779; F:actin binding; IDA. DR GO; GO:0017022; F:myosin binding; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0017137; F:Rab interactor activity; IDA. DR GO; GO:0030318; P:melanocyte differentiation; IMP. DR InterPro; IPR011011; FYVE_PHD_ZnF. DR InterPro; IPR010911; Rab_binding. DR PROSITE; PS50916; RABBD; 1. KW Coiled coil; Metal-binding; Repeat; Zinc; Zinc-finger. FT DOMAIN 4 124 Rab-binding. FT ZN_FING 64 107 FYVE-type. FT DOMAIN 339 485 Coiled coil (Potential). FT CONFLICT 254 254 R -> H (in Ref. 1). FT CONFLICT 475 475 E -> Q (in Ref. 1). SQ SEQUENCE 590 AA; 65052 MW; C91444B16B8EFA1D CRC64; MGKRLDLSTL TDEEAEHVWA VVQRDFDLRR REEERLQGLK GKIQKESSKR ELLSDTAHLN ETHCARCLQP YRLLLNSRRQ CLECSLFVCK SCSHAHPEEQ GWLCDPCHLA RVVKIGSLEW YYQHVRARFK RFGSAKVIRS LCGRLQGGGG SEPSLEEGNG DSEQTDEDGD LDTEARDQPL NSKKKKRLLS FRDVDFEEDS DHLVQPCSQT LGLSSVPESA HSLQSLSGEP YSEDTTSLEP EGLEETGARA LGCRPSPEVQ PCSPLPSGED AHAELDSPAA SCKSAFGTTA MPGTDDVRGK HLPSQYLADV DTSDEDSIQG PRAASQHSKR RARTVPETQI LELNKRMSAV EHLLVHLENT VLPPSAQEPT VETHPSADTE EETLRRRLEE LTSNISGSST SSEDETKPDG TFLGGSPKVC TDTGHMETQE RNPRSPGNPA RPTKSTDEEL SEMEDRVAMT ASEVQQAESE ISDIESRIAA LRAAGLTVKP SGKPRRKSGI PIFLPRVTEK LDRIPKTPPA DPDDQAKMPK ATTAVPSLLR RKYSPSSQGV DSGSFDRKSV YRGSLTQRNP NGRRGTARHI FAKPVMAQQP //