MELPH_HUMAN
ID MELPH_HUMAN Reviewed; 600 AA.
AC Q9BV36; B3KSS2; B4DKW7; G5E9G5; Q9HA71;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Melanophilin;
DE AltName: Full=Exophilin-3;
DE AltName: Full=Slp homolog lacking C2 domains a;
DE Short=SlaC2-a;
DE AltName: Full=Synaptotagmin-like protein 2a;
GN Name=MLPH; Synonyms=SLAC2A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5), AND
RP VARIANTS ALA-374 AND SER-451.
RC TISSUE=Kidney, Mammary gland, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP MUTAGENESIS OF GLU-14; ARG-24 AND GLU-32, INTERACTION WITH MYO5A AND
RP RAB27A, AND FUNCTION.
RX PubMed=12062444; DOI=10.1016/s0014-5793(02)02634-0;
RA Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T.,
RA Izumi T.;
RT "Melanophilin directly links Rab27a and myosin Va through its distinct
RT coiled-coil regions.";
RL FEBS Lett. 517:233-238(2002).
RN [6]
RP VARIANT GS3 TRP-35.
RX PubMed=12897212; DOI=10.1172/jci200318264;
RA Menasche G., Ho C.H., Sanal O., Feldmann J., Tezcan I., Ersoy F.,
RA Houdusse A., Fischer A., de Saint Basile G.;
RT "Griscelli syndrome restricted to hypopigmentation results from a
RT melanophilin defect (GS3) or a MYO5A F-exon deletion (GS1).";
RL J. Clin. Invest. 112:450-456(2003).
CC -!- FUNCTION: Rab effector protein involved in melanosome transport. Serves
CC as link between melanosome-bound RAB27A and the motor protein MYO5A.
CC {ECO:0000269|PubMed:12062444}.
CC -!- SUBUNIT: Binds RAB27A that has been activated by GTP-binding via its N-
CC terminus. Binds MYO5A via its C-terminal coiled coil domain.
CC -!- INTERACTION:
CC Q9BV36; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-7042162, EBI-465781;
CC Q9BV36; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-7042162, EBI-747505;
CC Q9BV36; P51159: RAB27A; NbExp=4; IntAct=EBI-7042162, EBI-716881;
CC Q9BV36; P51159-1: RAB27A; NbExp=2; IntAct=EBI-7042162, EBI-15528760;
CC Q9BV36; O00194: RAB27B; NbExp=3; IntAct=EBI-7042162, EBI-10179046;
CC Q9BV36; Q6P9E2: RECK; NbExp=3; IntAct=EBI-7042162, EBI-10253121;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BV36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BV36-2; Sequence=VSP_007554;
CC Name=3;
CC IsoId=Q9BV36-3; Sequence=VSP_042158, VSP_007554, VSP_042159;
CC Name=4;
CC IsoId=Q9BV36-4; Sequence=VSP_054367, VSP_054368;
CC Name=5;
CC IsoId=Q9BV36-5; Sequence=VSP_055730;
CC -!- DISEASE: Griscelli syndrome 3 (GS3) [MIM:609227]: Rare autosomal
CC recessive disorder characterized by pigmentary dilution of the skin and
CC hair, the presence of large clumps of pigment in hair shafts, and an
CC accumulation of melanosomes in melanocytes, without other clinical
CC manifestations. {ECO:0000269|PubMed:12897212}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=MLPHbase; Note=MLPH mutation db;
CC URL="http://structure.bmc.lu.se/idbase/MLPHbase/";
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DR EMBL; AK022207; BAB13984.1; -; mRNA.
DR EMBL; AK094168; BAG52834.1; -; mRNA.
DR EMBL; AK296745; BAG59329.1; -; mRNA.
DR EMBL; AK225381; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC104667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW71112.1; -; Genomic_DNA.
DR EMBL; BC001653; AAH01653.1; -; mRNA.
DR EMBL; BC051269; AAH51269.1; -; mRNA.
DR CCDS; CCDS2518.1; -. [Q9BV36-1]
DR CCDS; CCDS42836.1; -. [Q9BV36-2]
DR CCDS; CCDS63172.1; -. [Q9BV36-5]
DR CCDS; CCDS63173.1; -. [Q9BV36-3]
DR RefSeq; NP_001035932.1; NM_001042467.2. [Q9BV36-2]
DR RefSeq; NP_001268402.1; NM_001281473.1. [Q9BV36-3]
DR RefSeq; NP_001268403.1; NM_001281474.1. [Q9BV36-5]
DR RefSeq; NP_077006.1; NM_024101.6. [Q9BV36-1]
DR AlphaFoldDB; Q9BV36; -.
DR SMR; Q9BV36; -.
DR BioGRID; 122531; 17.
DR DIP; DIP-44046N; -.
DR IntAct; Q9BV36; 15.
DR MINT; Q9BV36; -.
DR STRING; 9606.ENSP00000264605; -.
DR iPTMnet; Q9BV36; -.
DR PhosphoSitePlus; Q9BV36; -.
DR BioMuta; MLPH; -.
DR DMDM; 32129730; -.
DR EPD; Q9BV36; -.
DR jPOST; Q9BV36; -.
DR MassIVE; Q9BV36; -.
DR MaxQB; Q9BV36; -.
DR PaxDb; Q9BV36; -.
DR PeptideAtlas; Q9BV36; -.
DR PRIDE; Q9BV36; -.
DR ProteomicsDB; 33931; -.
DR ProteomicsDB; 4492; -.
DR ProteomicsDB; 79162; -. [Q9BV36-1]
DR ProteomicsDB; 79163; -. [Q9BV36-2]
DR ProteomicsDB; 79164; -. [Q9BV36-3]
DR ABCD; Q9BV36; 3 sequenced antibodies.
DR Antibodypedia; 20264; 256 antibodies from 29 providers.
DR DNASU; 79083; -.
DR Ensembl; ENST00000264605.8; ENSP00000264605.3; ENSG00000115648.14. [Q9BV36-1]
DR Ensembl; ENST00000338530.8; ENSP00000341845.4; ENSG00000115648.14. [Q9BV36-2]
DR Ensembl; ENST00000409373.5; ENSP00000386780.1; ENSG00000115648.14. [Q9BV36-3]
DR Ensembl; ENST00000410032.5; ENSP00000386338.1; ENSG00000115648.14. [Q9BV36-5]
DR GeneID; 79083; -.
DR KEGG; hsa:79083; -.
DR MANE-Select; ENST00000264605.8; ENSP00000264605.3; NM_024101.7; NP_077006.1.
DR UCSC; uc002vws.4; human. [Q9BV36-1]
DR CTD; 79083; -.
DR DisGeNET; 79083; -.
DR GeneCards; MLPH; -.
DR HGNC; HGNC:29643; MLPH.
DR HPA; ENSG00000115648; Tissue enhanced (prostate, salivary gland).
DR MalaCards; MLPH; -.
DR MIM; 606526; gene.
DR MIM; 609227; phenotype.
DR neXtProt; NX_Q9BV36; -.
DR OpenTargets; ENSG00000115648; -.
DR Orphanet; 79478; Griscelli syndrome type 3.
DR PharmGKB; PA134899891; -.
DR VEuPathDB; HostDB:ENSG00000115648; -.
DR eggNOG; ENOG502RJPZ; Eukaryota.
DR GeneTree; ENSGT00950000183138; -.
DR HOGENOM; CLU_025193_2_0_1; -.
DR InParanoid; Q9BV36; -.
DR OMA; RISAVEC; -.
DR PhylomeDB; Q9BV36; -.
DR TreeFam; TF331599; -.
DR PathwayCommons; Q9BV36; -.
DR SignaLink; Q9BV36; -.
DR BioGRID-ORCS; 79083; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; MLPH; human.
DR GeneWiki; Melanophilin; -.
DR GenomeRNAi; 79083; -.
DR Pharos; Q9BV36; Tbio.
DR PRO; PR:Q9BV36; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BV36; protein.
DR Bgee; ENSG00000115648; Expressed in pancreatic ductal cell and 155 other tissues.
DR ExpressionAtlas; Q9BV36; baseline and differential.
DR Genevisible; Q9BV36; HS.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032402; P:melanosome transport; NAS:UniProtKB.
DR CDD; cd15752; FYVE_SlaC2-a; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR037442; Melanophilin_FYVE-rel_dom.
DR InterPro; IPR006788; Myrip/Melanophilin.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF04698; Rab_eff_C; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Disease variant;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..600
FT /note="Melanophilin"
FT /id="PRO_0000190222"
FT DOMAIN 4..124
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT ZN_FING 64..107
FT /note="FYVE-type"
FT REGION 146..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..496
FT /evidence="ECO:0000255"
FT COMPBIAS 202..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 186..225
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042158"
FT VAR_SEQ 226..368
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055730"
FT VAR_SEQ 341..368
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007554"
FT VAR_SEQ 430..481
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042159"
FT VAR_SEQ 514..551
FT /note="IFLPRVAGKLGKRPEDPNADPSSEAKAMAVPYLLRRKF -> ALYEGTLSLC
FT SEDLKHTHPDSVKSKRSRLNHVASCGNP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054367"
FT VAR_SEQ 552..600
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054368"
FT VARIANT 35
FT /note="R -> W (in GS3; abolishes RAB27A binding;
FT dbSNP:rs119473031)"
FT /evidence="ECO:0000269|PubMed:12897212"
FT /id="VAR_018724"
FT VARIANT 139
FT /note="R -> W (in dbSNP:rs2292880)"
FT /id="VAR_015690"
FT VARIANT 153
FT /note="L -> P (in dbSNP:rs3751109)"
FT /id="VAR_015691"
FT VARIANT 163
FT /note="D -> N (in dbSNP:rs3751108)"
FT /id="VAR_015692"
FT VARIANT 172
FT /note="G -> D (in dbSNP:rs3751107)"
FT /id="VAR_015693"
FT VARIANT 289
FT /note="T -> I (in dbSNP:rs11883500)"
FT /id="VAR_038410"
FT VARIANT 347
FT /note="H -> R (in dbSNP:rs2292884)"
FT /id="VAR_015694"
FT VARIANT 374
FT /note="V -> A (in dbSNP:rs3817362)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_015695"
FT VARIANT 451
FT /note="P -> S (in dbSNP:rs58256353)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061754"
FT MUTAGEN 14
FT /note="E->A: Abolishes RAB27A binding."
FT /evidence="ECO:0000269|PubMed:12062444"
FT MUTAGEN 24
FT /note="R->A: Decreases RAB27A binding."
FT /evidence="ECO:0000269|PubMed:12062444"
FT MUTAGEN 32
FT /note="E->A: Abolishes RAB27A binding."
FT /evidence="ECO:0000269|PubMed:12062444"
FT CONFLICT 109
FT /note="L -> P (in Ref. 1; BAB13984)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="G -> R (in Ref. 1; BAG52834)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="G -> R (in Ref. 1; AK225381)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="Q -> R (in Ref. 1; BAB13984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 65949 MW; 90F48D0B3250AD98 CRC64;
MGKKLDLSKL TDEEAQHVLE VVQRDFDLRR KEEERLEALK GKIKKESSKR ELLSDTAHLN
ETHCARCLQP YQLLVNSKRQ CLECGLFTCK SCGRVHPEEQ GWICDPCHLA RVVKIGSLEW
YYEHVKARFK RFGSAKVIRS LHGRLQGGAG PELISEERSG DSDQTDEDGE PGSEAQAQAQ
PFGSKKKRLL SVHDFDFEGD SDDSTQPQGH SLHLSSVPEA RDSPQSLTDE SCSEKAAPHK
AEGLEEADTG ASGCHSHPEE QPTSISPSRH GALAELCPPG GSHRMALGTA AALGSNVIRN
EQLPLQYLAD VDTSDEESIR AHVMASHHSK RRGRASSESQ IFELNKHISA VECLLTYLEN
TVVPPLAKGL GAGVRTEADV EEEALRRKLE ELTSNVSDQE TSSEEEEAKD EKAEPNRDKS
VGPLPQADPE VGTAAHQTNR QEKSPQDPGD PVQYNRTTDE ELSELEDRVA VTASEVQQAE
SEVSDIESRI AALRAAGLTV KPSGKPRRKS NLPIFLPRVA GKLGKRPEDP NADPSSEAKA
MAVPYLLRRK FSNSLKSQGK DDDSFDRKSV YRGSLTQRNP NARKGMASHT FAKPVVAHQS
