ID MELPH_MOUSE Reviewed; 590 AA. AC Q91V27; Q3UFV7; Q99N53; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 15-DEC-2009, entry version 66. DE RecName: Full=Melanophilin; DE AltName: Full=Exophilin-3; DE AltName: Full=Leaden protein; DE AltName: Full=Synaptotagmin-like protein 2a; DE AltName: Full=Slp homolog lacking C2 domains a; DE Short=SlaC2-a; GN Name=Mlph; Synonyms=Ln, Slac2a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 NUCLEOTIDE SEQUENCE [MRNA]. 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Melanoma; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). 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). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; THR-165; SER-313; RP SER-445; THR-446 AND SER-544, AND MASS SPECTROMETRY. RX PubMed=18973353; DOI=10.1021/pr800599n; RA Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., RA Faessler R., Mann M.; RT "Solid tumor proteome and phosphoproteome analysis by high resolution RT mass spectrometry."; RL J. Proteome Res. 7:5314-5326(2008). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-146 IN COMPLEX WITH RAB27B. RX PubMed=18940604; DOI=10.1016/j.str.2008.07.014; RA Kukimoto-Niino M., Sakamoto A., Kanno E., Hanawa-Suetsugu K., RA Terada T., Shirouzu M., Fukuda M., Yokoyama S.; RT "Structural basis for the exclusive specificity of Slac2- RT a/melanophilin for the Rab27 GTPases."; RL Structure 16:1478-1490(2008). 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 -!- INTERACTION: CC Q9ERI2:Rab27a; NbExp=1; IntAct=EBI-398308, EBI-398172; CC -!- SUBCELLULAR LOCATION: Melanosome. 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 RabBD (Rab-binding) 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; -; mRNA. DR EMBL; AF384098; AAK97435.1; -; mRNA. DR EMBL; AK148274; BAE28452.1; -; mRNA. DR IPI; IPI00320918; -. DR RefSeq; NP_443748.2; -. DR UniGene; Mm.105208; -. DR PDB; 2ZET; X-ray; 3.00 A; C/D=1-146. DR PDBsum; 2ZET; -. DR DIP; DIP-31495N; -. DR IntAct; Q91V27; 1. DR STRING; Q91V27; -. DR PhosphoSite; Q91V27; -. DR PRIDE; Q91V27; -. DR Ensembl; ENSMUST00000027528; ENSMUSP00000027528; ENSMUSG00000026303; Mus musculus. DR GeneID; 171531; -. DR KEGG; mmu:171531; -. DR UCSC; uc007bzm.1; mouse. DR CTD; 171531; -. DR MGI; MGI:2176380; Mlph. DR HOGENOM; HBG715136; -. DR HOVERGEN; Q91V27; -. DR InParanoid; Q91V27; -. DR NextBio; 371036; -. DR ArrayExpress; Q91V27; -. DR Bgee; Q91V27; -. DR CleanEx; MM_MLPH; -. DR Genevestigator; Q91V27; -. DR GermOnline; ENSMUSG00000026303; Mus musculus. DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI. DR GO; GO:0042470; C:melanosome; IDA:MGI. DR GO; GO:0003779; F:actin binding; IDA:MGI. DR GO; GO:0051010; F:microtubule plus-end binding; IPI:MGI. DR GO; GO:0031489; F:myosin V binding; IPI:MGI. DR GO; GO:0017137; F:Rab GTPase binding; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI. DR GO; GO:0032400; P:melanosome localization; IMP:MGI. DR GO; GO:0006605; P:protein targeting; IMP:MGI. DR InterPro; IPR006788; Myelin-assoc_OBP. DR InterPro; IPR010911; Rab_bd_domain. DR InterPro; IPR011011; Znf_FYVE_PHD. DR Pfam; PF04698; MOBP; 1. DR PROSITE; PS50916; RABBD; 1. DR PROSITE; PS50178; ZF_FYVE; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Metal-binding; Phosphoprotein; Repeat; KW Zinc; Zinc-finger. FT CHAIN 1 590 Melanophilin. FT /FTId=PRO_0000190223. FT DOMAIN 4 124 RabBD. FT ZN_FING 64 107 FYVE-type. FT COILED 339 485 Potential. FT MOD_RES 162 162 Phosphoserine. FT MOD_RES 165 165 Phosphothreonine. FT MOD_RES 313 313 Phosphoserine. FT MOD_RES 445 445 Phosphoserine. FT MOD_RES 446 446 Phosphothreonine. FT MOD_RES 544 544 Phosphoserine. FT CONFLICT 192 192 R -> Q (in Ref. 3; BAE28452). FT CONFLICT 254 254 R -> H (in Ref. 1; BAB41087). FT CONFLICT 333 333 R -> W (in Ref. 3; BAE28452). FT CONFLICT 360 360 T -> R (in Ref. 3; BAE28452). FT CONFLICT 475 475 E -> Q (in Ref. 1; BAB41087). FT CONFLICT 499 499 G -> S (in Ref. 3; BAE28452). FT HELIX 12 36 FT HELIX 43 53 FT HELIX 59 61 FT TURN 65 67 FT HELIX 71 73 FT TURN 82 84 FT HELIX 90 92 FT HELIX 105 114 FT HELIX 119 126 FT HELIX 135 140 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 //