PLSI_HUMAN
ID PLSI_HUMAN Reviewed; 629 AA.
AC Q14651; A8K2Q1; D3DNG3; Q8NEG6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Plastin-1;
DE AltName: Full=Intestine-specific plastin;
DE Short=I-plastin;
GN Name=PLS1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=8139549; DOI=10.1128/mcb.14.4.2457-2467.1994;
RA Lin C.-S., Shen W., Chen Z.P., Tu Y.-H., Matsudaira P.;
RT "Identification of I-plastin, a human fimbrin isoform expressed in
RT intestine and kidney.";
RL Mol. Cell. Biol. 14:2457-2467(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP INVOLVEMENT IN DFNA76, AND VARIANT DFNA76 LYS-269.
RX PubMed=31432506; DOI=10.1111/cge.13626;
RA Diaz-Horta O., Bademci G., Tokgoz-Yilmaz S., Guo S., Zafeer F.,
RA Sineni C.J., Duman D., Farooq A., Tekin M.;
RT "Novel variant p.E269K confirms causative role of PLS1 mutations in
RT autosomal dominant hearing loss.";
RL Clin. Genet. 96:575-578(2019).
RN [9]
RP INVOLVEMENT IN DFNA76, AND VARIANT DFNA76 PHE-363.
RX PubMed=30872814; DOI=10.1038/s41431-019-0372-y;
RA Schrauwen I., Melegh B.I., Chakchouk I., Acharya A., Nasir A., Poston A.,
RA Cornejo-Sanchez D.M., Szabo Z., Karosi T., Bene J., Melegh B., Leal S.M.;
RT "Hearing impairment locus heterogeneity and identification of PLS1 as a new
RT autosomal dominant gene in Hungarian Roma.";
RL Eur. J. Hum. Genet. 27:869-878(2019).
RN [10]
RP INVOLVEMENT IN DFNA76, AND VARIANTS DFNA76 SER-128; ARG-238 AND LYS-269.
RX PubMed=31397523; DOI=10.1002/humu.23891;
RA Morgan A., Koboldt D.C., Barrie E.S., Crist E.R., Garcia Garcia G.,
RA Mezzavilla M., Faletra F., Mihalic Mosher T., Wilson R.K., Blanchet C.,
RA Manickam K., Roux A.F., Gasparini P., Dell'Orco D., Girotto G.;
RT "Mutations in PLS1, encoding fimbrin, cause autosomal dominant nonsyndromic
RT hearing loss.";
RL Hum. Mutat. 40:2286-2295(2019).
CC -!- FUNCTION: Actin-bundling protein. In the inner ear, it is required for
CC stereocilia formation. Mediates liquid packing of actin filaments that
CC is necessary for stereocilia to grow to their proper dimensions.
CC {ECO:0000250|UniProtKB:Q3V0K9}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3V0K9}. Cell
CC projection, stereocilium {ECO:0000250|UniProtKB:Q3V0K9}.
CC -!- TISSUE SPECIFICITY: In small intestine, colon, and kidney; relatively
CC lower levels of expression are detected in the lung and stomach.
CC {ECO:0000269|PubMed:8139549}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISEASE: Deafness, autosomal dominant, 76 (DFNA76) [MIM:618787]: A form
CC of non-syndromic deafness characterized by mild to profound
CC sensorineural hearing loss and variable age at onset. Sensorineural
CC hearing loss results from damage to the neural receptors of the inner
CC ear, the nerve pathways to the brain, or the area of the brain that
CC receives sound information. {ECO:0000269|PubMed:30872814,
CC ECO:0000269|PubMed:31397523, ECO:0000269|PubMed:31432506}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; L20826; AAA19869.1; -; mRNA.
DR EMBL; AK290316; BAF83005.1; -; mRNA.
DR EMBL; CH471052; EAW78965.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78967.1; -; Genomic_DNA.
DR EMBL; BC031083; AAH31083.1; -; mRNA.
DR CCDS; CCDS3125.1; -.
DR PIR; A56536; A56536.
DR RefSeq; NP_001138791.1; NM_001145319.1.
DR RefSeq; NP_001165783.1; NM_001172312.1.
DR RefSeq; NP_002661.2; NM_002670.2.
DR RefSeq; XP_006713723.1; XM_006713660.3.
DR RefSeq; XP_011511202.1; XM_011512900.2.
DR RefSeq; XP_011511203.1; XM_011512901.1.
DR RefSeq; XP_011511205.1; XM_011512903.2.
DR RefSeq; XP_016862115.1; XM_017006626.1.
DR RefSeq; XP_016862116.1; XM_017006627.1.
DR AlphaFoldDB; Q14651; -.
DR SMR; Q14651; -.
DR BioGRID; 111371; 133.
DR IntAct; Q14651; 41.
DR MINT; Q14651; -.
DR STRING; 9606.ENSP00000336831; -.
DR GlyGen; Q14651; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q14651; -.
DR MetOSite; Q14651; -.
DR PhosphoSitePlus; Q14651; -.
DR BioMuta; PLS1; -.
DR DMDM; 224471848; -.
DR EPD; Q14651; -.
DR jPOST; Q14651; -.
DR MassIVE; Q14651; -.
DR MaxQB; Q14651; -.
DR PaxDb; Q14651; -.
DR PeptideAtlas; Q14651; -.
DR PRIDE; Q14651; -.
DR ProteomicsDB; 60090; -.
DR Antibodypedia; 33495; 155 antibodies from 25 providers.
DR DNASU; 5357; -.
DR Ensembl; ENST00000337777.7; ENSP00000336831.3; ENSG00000120756.13.
DR Ensembl; ENST00000457734.7; ENSP00000387890.2; ENSG00000120756.13.
DR Ensembl; ENST00000497002.1; ENSP00000418700.1; ENSG00000120756.13.
DR GeneID; 5357; -.
DR KEGG; hsa:5357; -.
DR MANE-Select; ENST00000457734.7; ENSP00000387890.2; NM_001145319.2; NP_001138791.1.
DR UCSC; uc003euz.4; human.
DR CTD; 5357; -.
DR DisGeNET; 5357; -.
DR GeneCards; PLS1; -.
DR HGNC; HGNC:9090; PLS1.
DR HPA; ENSG00000120756; Tissue enriched (intestine).
DR MalaCards; PLS1; -.
DR MIM; 602734; gene.
DR MIM; 618787; phenotype.
DR neXtProt; NX_Q14651; -.
DR OpenTargets; ENSG00000120756; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA33417; -.
DR VEuPathDB; HostDB:ENSG00000120756; -.
DR eggNOG; KOG0046; Eukaryota.
DR GeneTree; ENSGT00950000183097; -.
DR HOGENOM; CLU_015284_2_0_1; -.
DR InParanoid; Q14651; -.
DR OMA; KDDPDCK; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; Q14651; -.
DR TreeFam; TF300680; -.
DR PathwayCommons; Q14651; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q14651; -.
DR BioGRID-ORCS; 5357; 15 hits in 1080 CRISPR screens.
DR GenomeRNAi; 5357; -.
DR Pharos; Q14651; Tbio.
DR PRO; PR:Q14651; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14651; protein.
DR Bgee; ENSG00000120756; Expressed in secondary oocyte and 158 other tissues.
DR ExpressionAtlas; Q14651; baseline and differential.
DR Genevisible; Q14651; HS.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR GO; GO:1990357; C:terminal web; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR GO; GO:0001951; P:intestinal D-glucose absorption; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0032532; P:regulation of microvillus length; IEA:Ensembl.
DR GO; GO:1902896; P:terminal web assembly; IEA:Ensembl.
DR GO; GO:0060121; P:vestibular receptor cell stereocilium organization; ISS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR InterPro; IPR030235; PLS1.
DR PANTHER; PTHR19961; PTHR19961; 1.
DR PANTHER; PTHR19961:SF27; PTHR19961:SF27; 1.
DR Pfam; PF00307; CH; 4.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00033; CH; 4.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 2.
DR PROSITE; PS00020; ACTININ_2; 2.
DR PROSITE; PS50021; CH; 4.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Calcium; Cell projection; Cytoplasm; Deafness;
KW Disease variant; Metal-binding; Non-syndromic deafness; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..629
FT /note="Plastin-1"
FT /id="PRO_0000073750"
FT DOMAIN 11..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 51..86
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 122..238
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 266..376
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 395..504
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 516..625
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 108..380
FT /note="Actin-binding 1"
FT REGION 381..625
FT /note="Actin-binding 2"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 128
FT /note="F -> S (in DFNA76)"
FT /evidence="ECO:0000269|PubMed:31397523"
FT /id="VAR_083821"
FT VARIANT 146
FT /note="I -> M (in dbSNP:rs35710125)"
FT /id="VAR_048660"
FT VARIANT 216
FT /note="S -> L (in dbSNP:rs35435507)"
FT /id="VAR_048661"
FT VARIANT 238
FT /note="L -> R (in DFNA76)"
FT /evidence="ECO:0000269|PubMed:31397523"
FT /id="VAR_083822"
FT VARIANT 269
FT /note="E -> K (in DFNA76)"
FT /evidence="ECO:0000269|PubMed:31397523,
FT ECO:0000269|PubMed:31432506"
FT /id="VAR_083823"
FT VARIANT 363
FT /note="L -> F (in DFNA76)"
FT /evidence="ECO:0000269|PubMed:30872814"
FT /id="VAR_083824"
FT CONFLICT 317
FT /note="P -> L (in Ref. 2; BAF83005)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="S -> R (in Ref. 4; AAH31083)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="G -> R (in Ref. 1; AAA19869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 70253 MW; F904031933C2C323 CRC64;
MENSTTTISR EELEELQEAF NKIDIDNSGY VSDYELQDLF KEASLPLPGY KVREIVEKIL
SVADSNKDGK ISFEEFVSLM QELKSKDISK TFRKIINKRE GITAIGGTST ISSEGTQHSY
SEEEKVAFVN WINKALENDP DCKHLIPMNP NDDSLFKSLA DGILLCKMIN LSEPDTIDER
AINKKKLTPF TISENLNLAL NSASAIGCTV VNIGASDLKE GKPHLVLGLL WQIIKVGLFA
DIEISRNEAL IALLNEGEEL EELMKLSPEE LLLRWVNYHL TNAGWHTISN FSQDIKDSRA
YFHLLNQIAP KGGEDGPAIA IDLSGINETN DLKRAGLMLQ EADKLGCKQF VTPADVVSGN
PKLNLAFVAN LFNTYPCLHK PNNNDIDMNL LEGESKEERT FRNWMNSLGV NPYINHLYSD
LADALVIFQL YEMIRVPVNW SHVNKPPYPA LGGNMKKIEN CNYAVELGKN KAKFSLVGIA
GQDLNEGNST LTLALVWQLM RRYTLNVLSD LGEGEKVNDE IIIKWVNQTL KSANKKTSIS
SFKDKSISTS LPVLDLIDAI APNAVRQEMI RRENLSDEDK LNNAKYAISV ARKIGARIYA
LPDDLVEVKP KMVMTVFACL MGKGLNRIK
