ARMX3_HUMAN
ID ARMX3_HUMAN Reviewed; 379 AA.
AC Q9UH62; Q53HC6; Q7LCF5; Q9NPE4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Armadillo repeat-containing X-linked protein 3;
DE AltName: Full=ARM protein lost in epithelial cancers on chromosome X 3;
DE Short=Protein ALEX3;
GN Name=ARMCX3; Synonyms=ALEX3; ORFNames=BM-017, UNQ2517/PRO6007;
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].
RC TISSUE=Testis;
RX PubMed=11162520; DOI=10.1006/bbrc.2000.4125;
RA Kurochkin I.V., Yonemitsu N., Funahashi S., Nomura H.;
RT "ALEX1, a novel human armadillo repeat protein that is expressed
RT differentially in normal tissues and carcinomas.";
RL Biochem. Biophys. Res. Commun. 280:340-347(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Nicolas G., Galand C., Lecomte M.-C.;
RT "Identification of a new protein as a putative binding partner of SH3
RT domain of non-erythroid alpha-spectrin (alpha-fodrin).";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-67, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-72 AND SER-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Regulates mitochondrial aggregation and transport in axons in
CC living neurons. May link mitochondria to the TRAK2-kinesin motor
CC complex via its interaction with Miro and TRAK2. Mitochondrial
CC distribution and dynamics is regulated through ARMCX3 protein
CC degradation, which is promoted by PCK and negatively regulated by WNT1.
CC Enhances the SOX10-mediated transactivation of the neuronal
CC acetylcholine receptor subunit alpha-3 and beta-4 subunit gene
CC promoters. {ECO:0000250|UniProtKB:Q8BHS6}.
CC -!- SUBUNIT: Interacts (via ARM domain) with MIRO1, MIRO2 and TRAK2. The
CC interaction with Miro is calcium-dependent. Interacts with SOX10.
CC {ECO:0000250|UniProtKB:Q8BHS6}.
CC -!- INTERACTION:
CC Q9UH62; Q08426: EHHADH; NbExp=3; IntAct=EBI-717832, EBI-2339219;
CC Q9UH62; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-717832, EBI-14240149;
CC Q9UH62; Q9H063: MAF1; NbExp=3; IntAct=EBI-717832, EBI-720354;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8BHS6}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8BHS6}. Nucleus
CC {ECO:0000250|UniProtKB:Q8BHS6}.
CC -!- SIMILARITY: Belongs to the eutherian X-chromosome-specific Armcx
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ALEX3Xq22ID479.html";
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DR EMBL; AB039669; BAA94602.1; -; mRNA.
DR EMBL; AF211175; AAF24487.1; -; mRNA.
DR EMBL; AF208859; AAF64273.1; -; mRNA.
DR EMBL; AY359079; AAQ89438.1; -; mRNA.
DR EMBL; AK222655; BAD96375.1; -; mRNA.
DR EMBL; CR933656; CAI45955.1; -; mRNA.
DR EMBL; AL121883; CAI42939.1; -; Genomic_DNA.
DR EMBL; BC005194; AAH05194.1; -; mRNA.
DR CCDS; CCDS14489.1; -.
DR RefSeq; NP_057691.1; NM_016607.3.
DR RefSeq; NP_808816.1; NM_177947.2.
DR RefSeq; NP_808817.1; NM_177948.2.
DR RefSeq; XP_005262198.1; XM_005262141.2.
DR AlphaFoldDB; Q9UH62; -.
DR SMR; Q9UH62; -.
DR BioGRID; 119614; 126.
DR IntAct; Q9UH62; 28.
DR MINT; Q9UH62; -.
DR STRING; 9606.ENSP00000340672; -.
DR iPTMnet; Q9UH62; -.
DR MetOSite; Q9UH62; -.
DR PhosphoSitePlus; Q9UH62; -.
DR BioMuta; ARMCX3; -.
DR DMDM; 74753322; -.
DR EPD; Q9UH62; -.
DR jPOST; Q9UH62; -.
DR MassIVE; Q9UH62; -.
DR MaxQB; Q9UH62; -.
DR PaxDb; Q9UH62; -.
DR PeptideAtlas; Q9UH62; -.
DR PRIDE; Q9UH62; -.
DR ProteomicsDB; 84277; -.
DR Antibodypedia; 378; 247 antibodies from 29 providers.
DR DNASU; 51566; -.
DR Ensembl; ENST00000341189.8; ENSP00000340672.4; ENSG00000102401.20.
DR Ensembl; ENST00000471229.7; ENSP00000454483.1; ENSG00000102401.20.
DR Ensembl; ENST00000537169.1; ENSP00000439032.1; ENSG00000102401.20.
DR GeneID; 51566; -.
DR KEGG; hsa:51566; -.
DR MANE-Select; ENST00000471229.7; ENSP00000454483.1; NM_177947.3; NP_808816.1.
DR UCSC; uc004ehz.2; human.
DR CTD; 51566; -.
DR DisGeNET; 51566; -.
DR GeneCards; ARMCX3; -.
DR HGNC; HGNC:24065; ARMCX3.
DR HPA; ENSG00000102401; Low tissue specificity.
DR MIM; 300364; gene.
DR neXtProt; NX_Q9UH62; -.
DR OpenTargets; ENSG00000102401; -.
DR PharmGKB; PA134977725; -.
DR VEuPathDB; HostDB:ENSG00000102401; -.
DR eggNOG; ENOG502TCDI; Eukaryota.
DR GeneTree; ENSGT00940000162753; -.
DR HOGENOM; CLU_037187_0_0_1; -.
DR InParanoid; Q9UH62; -.
DR OMA; DSKSIVW; -.
DR OrthoDB; 860703at2759; -.
DR PhylomeDB; Q9UH62; -.
DR TreeFam; TF335652; -.
DR PathwayCommons; Q9UH62; -.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR SignaLink; Q9UH62; -.
DR BioGRID-ORCS; 51566; 11 hits in 702 CRISPR screens.
DR ChiTaRS; ARMCX3; human.
DR GeneWiki; ARMCX3; -.
DR GenomeRNAi; 51566; -.
DR Pharos; Q9UH62; Tdark.
DR PRO; PR:Q9UH62; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9UH62; protein.
DR Bgee; ENSG00000102401; Expressed in lateral nuclear group of thalamus and 204 other tissues.
DR ExpressionAtlas; Q9UH62; baseline and differential.
DR Genevisible; Q9UH62; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR006911; ARM-rpt_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR Pfam; PF04826; Arm_2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..379
FT /note="Armadillo repeat-containing X-linked protein 3"
FT /id="PRO_0000191366"
FT TOPO_DOM 1..6
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q8BHS6"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BHS6"
FT REPEAT 111..151
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 153..192
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 233..272
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REGION 1..6
FT /note="Mitochondrion outer membrane (MOM)-targeting
FT sequence"
FT /evidence="ECO:0000305"
FT REGION 26..37
FT /note="Mitochondrion outer membrane (MOM)-targeting
FT sequence"
FT /evidence="ECO:0000305"
FT REGION 89..98
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q8BHS6"
FT REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 310
FT /note="E -> V (in Ref. 5; BAD96375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42501 MW; B715D7F83DF4DFB0 CRC64;
MGYARKVGWV TAGLVIGAGA CYCIYRLTRG RKQNKEKMAE GGSGDVDDAG DCSGARYNDW
SDDDDDSNES KSIVWYPPWA RIGTEAGTRA RARARARATR ARRAVQKRAS PNSDDTVLSP
QELQKVLCLV EMSEKPYILE AALIALGNNA AYAFNRDIIR DLGGLPIVAK ILNTRDPIVK
EKALIVLNNL SVNAENQRRL KVYMNQVCDD TITSRLNSSV QLAGLRLLTN MTVTNEYQHM
LANSISDFFR LFSAGNEETK LQVLKLLLNL AENPAMTREL LRAQVPSSLG SLFNKKENKE
VILKLLVIFE NINDNFKWEE NEPTQNQFGE GSLFFFLKEF QVCADKVLGI ESHHDFLVKV
KVGKFMAKLA EHMFPKSQE
