| General information | | DisProt: | DP00541 | | Name: | Melanophilin | | Synonym(s): | MELPH_MOUSE
Exophilin-3
Leaden protein
Synaptotagmin-like protein 2a
Slp homolog lacking C2 domains a
SlaC2-a
| | First appeared in release: | Release 3.7 (01/28/2008) | | UniProt: | Q91V27 | | UniGene: | Mm.105208 | | SwissProt: | MELPH_MOUSE | | TrEMBL: | | | NCBI (GI): | 32129728 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 590 | | Percent disordered: | 44% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MGKRLDLSTL TDEEAEHVWA VVQRDFDLRR REEERLQGLK GKIQKESSKR ELLSDTAHLN - 60
ETHCARCLQP YRLLLNSRRQ CLECSLFVCK SCSHAHPEEQ GWLCDPCHLA RVVKIGSLEW - 120
YYQHVRARFK RFGSAKVIRS LCGRLQGGGG SEPSLEEGNG DSEQTDEDGD LDTEARDQPL - 180
NSKKKKRLLS FRDVDFEEDS DHLVQPCSQT LGLSSVPESA HSLQSLSGEP YSEDTTSLEP - 240
EGLEETGARA LGCRPSPEVQ PCSPLPSGED AHAELDSPAA SCKSAFGTTA MPGTDDVRGK - 300
HLPSQYLADV DTSDEDSIQG PRAASQHSKR RARTVPETQI LELNKRMSAV EHLLVHLENT - 360
VLPPSAQEPT VETHPSADTE EETLRRRLEE LTSNISGSST SSEDETKPDG TFLGGSPKVC - 420
TDTGHMETQE RNPRSPGNPA RPTKSTDEEL SEMEDRVAMT ASEVQQAESE ISDIESRIAA - 480
LRAAGLTVKP SGKPRRKSGI PIFLPRVTEK LDRIPKTPPA DPDDQAKMPK ATTAVPSLLR - 540
RKYSPSSQGV DSGSFDRKSV YRGSLTQRNP NGRRGTARHI FAKPVMAQQP
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| Functional narrative |
The proper peripheral distribution of melanosomes, a dense pigment-containing organelle, is dependent on actin and the activity of myosin Va. The recruitment of myosin Va to the melanosome and proper transport of the melanosome requires melanophilin, which directly binds to myosin Va and is tethered to the melanosome membrane via Rab27a. Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Myosin Va binding domain | | Location: | 147 - 403 | | Length: | 257 | | Region sequence: |
GGGGSEPSLEEGNGDSEQTDEDGDLDTEARDQPLNSKKKKRLLSFRDVDFEEDSDHLVQP
CSQTLGLSSVPESAHSLQSLSGEPYSEDTTSLEPEGLEETGARALGCRPSPEVQPCSPLP
SGEDAHAELDSPAASCKSAFGTTAMPGTDDVRGKHLPSQYLADVDTSDEDSIQGPRAASQ
HSKRRARTVPETQILELNKRMSAVEHLLVHLENTVLPPSAQEPTVETHPSADTEEETLRR
RLEELTSNISGSSTSSE | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | | | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.5; K2HPO4 20 mM)
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; NaCl 75 mM; NaH2PO4 20 mM)
- Sensitivity to proteolysis (277 K; pH: 8; DTT 1 mM; NaCl 150 mM; Tris-HCl 50 mM)
- Size exclusion/gel filtration chromatography (pH: 7.5; DTT 1 mM; HEPES-KOH 25 mM; NaCl 150 mM)
- Dynamic light scattering
| References:
- Geething NC, Spudich JA. "Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin." J Biol Chem. 2007; 282(29): 21518-28. PubMed: 17513864
| Comments:
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| References |
- Geething NC, Spudich JA. "Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin." J Biol Chem. 2007; 282(29): 21518-28. PubMed: 17513864
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