BL1S5_HUMAN
ID BL1S5_HUMAN Reviewed; 187 AA.
AC Q8TDH9; B4DVM2; Q0VDJ6; Q0VDJ7; Q5THS1; Q68D56; Q8N5F9; Q9NU16;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 5 {ECO:0000305};
DE Short=BLOC-1 subunit 5;
DE AltName: Full=Protein Muted homolog;
GN Name=BLOC1S5 {ECO:0000312|HGNC:HGNC:18561}; Synonyms=MUTED;
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 [MRNA] (ISOFORM 1).
RX PubMed=11912185; DOI=10.1093/hmg/11.6.697;
RA Zhang Q., Li W., Novak E.K., Karim A., Mishra V.S., Kingsmore S.F.,
RA Roe B.A., Suzuki T., Swank R.T.;
RT "The gene for the muted (mu) mouse, a model for Hermansky-Pudlak syndrome,
RT defines a novel protein which regulates vesicle trafficking.";
RL Hum. Mol. Genet. 11:697-706(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lymph;
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 [6]
RP INTERACTION WITH BLOC1S6.
RX PubMed=12191018; DOI=10.1034/j.1600-0854.2002.30908.x;
RA Moriyama K., Bonifacino J.S.;
RT "Pallidin is a component of a multi-protein complex involved in the
RT biogenesis of lysosome-related organelles.";
RL Traffic 3:666-677(2002).
RN [7]
RP INTERACTION WITH BLOC1S6.
RX PubMed=12019270; DOI=10.1074/jbc.m204011200;
RA Falcon-Perez J.M., Starcevic M., Gautam R., Dell'Angelica E.C.;
RT "BLOC-1, a novel complex containing the pallidin and muted proteins
RT involved in the biogenesis of melanosomes and platelet-dense granules.";
RL J. Biol. Chem. 277:28191-28199(2002).
RN [8]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND FUNCTION.
RX PubMed=17182842; DOI=10.1091/mbc.e06-12-1066;
RA Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C.,
RA Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
RA Dell'Angelica E.C., Raposo G., Marks M.S.;
RT "BLOC-1 is required for cargo-specific sorting from vacuolar early
RT endosomes toward lysosome-related organelles.";
RL Mol. Biol. Cell 18:768-780(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
RP COMPLEX.
RX PubMed=22203680; DOI=10.1074/jbc.m111.325746;
RA Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C.,
RA Bonifacino J.S., Hurley J.H.;
RT "Assembly and architecture of biogenesis of lysosome-related organelles
RT complex-1 (BLOC-1).";
RL J. Biol. Chem. 287:5882-5890(2012).
RN [12]
RP INVOLVED IN HPS11, AND FUNCTION.
RX PubMed=32565547; DOI=10.1038/s41436-020-0867-5;
RA Pennamen P., Le L., Tingaud-Sequeira A., Fiore M., Bauters A.,
RA Van Duong Beatrice N., Coste V., Bordet J.C., Plaisant C., Diallo M.,
RA Michaud V., Trimouille A., Lacombe D., Lasseaux E., Delevoye C.,
RA Picard F.M., Delobel B., Marks M.S., Arveiler B.;
RT "BLOC1S5 pathogenic variants cause a new type of Hermansky-Pudlak
RT syndrome.";
RL Genet. Med. 22:1613-1622(2020).
CC -!- FUNCTION: Component of the BLOC-1 complex, a complex that is required
CC for normal biogenesis of lysosome-related organelles (LRO), such as
CC platelet dense granules and melanosomes (PubMed:32565547). In concert
CC with the AP-3 complex, the BLOC-1 complex is required to target
CC membrane protein cargos into vesicles assembled at cell bodies for
CC delivery into neurites and nerve terminals. The BLOC-1 complex, in
CC association with SNARE proteins, is also proposed to be involved in
CC neurite extension. Plays a role in intracellular vesicle trafficking.
CC {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:32565547}.
CC -!- SUBUNIT: Interacts with BLOC1S4, DTNBP1/BLOC1S7 and PI4K2A (By
CC similarity). Component of the biogenesis of lysosome-related organelles
CC complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4,
CC BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed
CC of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with
CC the AP-3 protein complex and membrane protein cargos. Interacts with
CC BLOC1S6. {ECO:0000250, ECO:0000269|PubMed:12019270,
CC ECO:0000269|PubMed:12191018, ECO:0000269|PubMed:17182842,
CC ECO:0000269|PubMed:22203680}.
CC -!- INTERACTION:
CC Q8TDH9; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-465861, EBI-11096309;
CC Q8TDH9; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-465861, EBI-742038;
CC Q8TDH9; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-465861, EBI-465804;
CC Q8TDH9; O75506: HSBP1; NbExp=3; IntAct=EBI-465861, EBI-748664;
CC Q8TDH9; O43482: OIP5; NbExp=3; IntAct=EBI-465861, EBI-536879;
CC Q8TDH9; P40425: PBX2; NbExp=3; IntAct=EBI-465861, EBI-348489;
CC Q8TDH9; P55347: PKNOX1; NbExp=3; IntAct=EBI-465861, EBI-1373569;
CC Q8TDH9; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-465861, EBI-358489;
CC Q8TDH9; Q99598: TSNAX; NbExp=6; IntAct=EBI-465861, EBI-742638;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TDH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDH9-2; Sequence=VSP_015088, VSP_015089;
CC Name=3;
CC IsoId=Q8TDH9-3; Sequence=VSP_045013;
CC -!- DISEASE: Hermansky-Pudlak syndrome 11 (HPS11) [MIM:619172]: A form of
CC Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal
CC recessive disorder characterized by oculocutaneous albinism, bleeding
CC due to platelet storage pool deficiency, and lysosomal storage defects.
CC This syndrome results from defects of diverse cytoplasmic organelles
CC including melanosomes, platelet dense granules and lysosomes. Ceroid
CC storage in the lungs is associated with pulmonary fibrosis, a common
CC cause of premature death in individuals with HPS.
CC {ECO:0000269|PubMed:32565547}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the BLOC1S5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32438.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF426434; AAL99385.1; -; mRNA.
DR EMBL; AK301142; BAG62734.1; -; mRNA.
DR EMBL; CR749569; CAH18364.1; -; mRNA.
DR EMBL; AL023694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032438; AAH32438.1; ALT_INIT; mRNA.
DR EMBL; BC119644; AAI19645.1; -; mRNA.
DR EMBL; BC119645; AAI19646.1; -; mRNA.
DR CCDS; CCDS4506.1; -. [Q8TDH9-1]
DR RefSeq; NP_001186251.1; NM_001199322.1. [Q8TDH9-3]
DR RefSeq; NP_958437.1; NM_201280.2. [Q8TDH9-1]
DR AlphaFoldDB; Q8TDH9; -.
DR SMR; Q8TDH9; -.
DR BioGRID; 121986; 43.
DR ComplexPortal; CPX-1910; BLOC-1 complex.
DR CORUM; Q8TDH9; -.
DR IntAct; Q8TDH9; 20.
DR STRING; 9606.ENSP00000380598; -.
DR GlyGen; Q8TDH9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TDH9; -.
DR PhosphoSitePlus; Q8TDH9; -.
DR BioMuta; BLOC1S5; -.
DR DMDM; 34582369; -.
DR EPD; Q8TDH9; -.
DR jPOST; Q8TDH9; -.
DR MassIVE; Q8TDH9; -.
DR MaxQB; Q8TDH9; -.
DR PaxDb; Q8TDH9; -.
DR PeptideAtlas; Q8TDH9; -.
DR PRIDE; Q8TDH9; -.
DR ProteomicsDB; 58830; -.
DR ProteomicsDB; 74287; -. [Q8TDH9-1]
DR ProteomicsDB; 74288; -. [Q8TDH9-2]
DR Antibodypedia; 34994; 123 antibodies from 20 providers.
DR DNASU; 63915; -.
DR Ensembl; ENST00000397457.7; ENSP00000380598.2; ENSG00000188428.20. [Q8TDH9-1]
DR GeneID; 63915; -.
DR KEGG; hsa:63915; -.
DR MANE-Select; ENST00000397457.7; ENSP00000380598.2; NM_201280.3; NP_958437.1.
DR UCSC; uc003mxy.3; human. [Q8TDH9-1]
DR CTD; 63915; -.
DR DisGeNET; 63915; -.
DR GeneCards; BLOC1S5; -.
DR GeneReviews; BLOC1S5; -.
DR HGNC; HGNC:18561; BLOC1S5.
DR HPA; ENSG00000188428; Low tissue specificity.
DR MalaCards; BLOC1S5; -.
DR MIM; 607289; gene.
DR MIM; 619172; phenotype.
DR neXtProt; NX_Q8TDH9; -.
DR OpenTargets; ENSG00000188428; -.
DR Orphanet; 231531; Hermansky-Pudlak syndrome due to BLOC-1 deficiency.
DR PharmGKB; PA134921692; -.
DR VEuPathDB; HostDB:ENSG00000188428; -.
DR eggNOG; ENOG502S2QH; Eukaryota.
DR GeneTree; ENSGT00390000016974; -.
DR InParanoid; Q8TDH9; -.
DR OMA; IQWEDFM; -.
DR OrthoDB; 1593497at2759; -.
DR PhylomeDB; Q8TDH9; -.
DR TreeFam; TF332943; -.
DR PathwayCommons; Q8TDH9; -.
DR SignaLink; Q8TDH9; -.
DR SIGNOR; Q8TDH9; -.
DR BioGRID-ORCS; 63915; 7 hits in 1078 CRISPR screens.
DR GeneWiki; MUTED; -.
DR GenomeRNAi; 63915; -.
DR Pharos; Q8TDH9; Tbio.
DR PRO; PR:Q8TDH9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8TDH9; protein.
DR Bgee; ENSG00000188428; Expressed in pancreatic ductal cell and 196 other tissues.
DR ExpressionAtlas; Q8TDH9; baseline and differential.
DR Genevisible; Q8TDH9; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0035646; P:endosome to melanosome transport; IDA:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; IDA:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0032474; P:otolith morphogenesis; IEA:Ensembl.
DR GO; GO:0050942; P:positive regulation of pigment cell differentiation; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl.
DR InterPro; IPR017243; Bloc1s5.
DR PANTHER; PTHR31784; PTHR31784; 1.
DR Pfam; PF14942; Muted; 1.
DR PIRSF; PIRSF037610; BLOC-1_complex_muted_subunit; 1.
PE 1: Evidence at protein level;
KW Acetylation; Albinism; Alternative splicing; Coiled coil;
KW Hermansky-Pudlak syndrome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..187
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 5"
FT /id="PRO_0000096651"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 154..186
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..65
FT /note="MSGGGTETPVGCEAAPGGGSKKRDSLGTAGSAHLIIKDLGEIHSRLLDHRPV
FT IQGETRYFVKEFE -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045013"
FT VAR_SEQ 109..110
FT /note="LQ -> YS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015088"
FT VAR_SEQ 111..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015089"
SQ SEQUENCE 187 AA; 21609 MW; 790D4DE8E97D83D1 CRC64;
MSGGGTETPV GCEAAPGGGS KKRDSLGTAG SAHLIIKDLG EIHSRLLDHR PVIQGETRYF
VKEFEEKRGL REMRVLENLK NMIHETNEHT LPKCRDTMRD SLSQVLQRLQ AANDSVCRLQ
QREQERKKIH SDHLVASEKQ HMLQWDNFMK EQPNKRAEVD EEHRKAMERL KEQYAEMEKD
LAKFSTF
