MYO5C_HUMAN
ID MYO5C_HUMAN Reviewed; 1742 AA.
AC Q9NQX4; Q6P1W8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Unconventional myosin-Vc;
GN Name=MYO5C;
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), VARIANT PRO-522, AND TISSUE
RP SPECIFICITY.
RX PubMed=11870218; DOI=10.1242/jcs.115.5.991;
RA Rodriguez O.C., Cheney R.E.;
RT "Human myosin-Vc is a novel class V myosin expressed in epithelial cells.";
RL J. Cell Sci. 115:991-1004(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [4]
RP PROTEIN SEQUENCE OF 2-12, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
CC -!- FUNCTION: May be involved in transferrin trafficking. Likely to power
CC actin-based membrane trafficking in many physiologically crucial
CC tissues.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQX4-2; Sequence=VSP_056592, VSP_056593;
CC -!- TISSUE SPECIFICITY: Expressed chiefly in non-neuronal tissues.
CC Particularly abundant in epithelial and glandular tissues including
CC pancreas, prostate, mammary, stomach, colon and lung.
CC {ECO:0000269|PubMed:11870218}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF272390; AAF78783.1; -; mRNA.
DR EMBL; AC010674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064841; AAH64841.1; -; mRNA.
DR CCDS; CCDS42036.1; -. [Q9NQX4-1]
DR RefSeq; NP_061198.2; NM_018728.3. [Q9NQX4-1]
DR PDB; 4L8T; X-ray; 2.95 A; A=1319-1742.
DR PDB; 4ZG4; X-ray; 2.36 A; B/E=1-755.
DR PDB; 5HMP; X-ray; 2.40 A; A/B=5-754.
DR PDBsum; 4L8T; -.
DR PDBsum; 4ZG4; -.
DR PDBsum; 5HMP; -.
DR AlphaFoldDB; Q9NQX4; -.
DR SMR; Q9NQX4; -.
DR BioGRID; 121005; 180.
DR IntAct; Q9NQX4; 113.
DR STRING; 9606.ENSP00000261839; -.
DR iPTMnet; Q9NQX4; -.
DR PhosphoSitePlus; Q9NQX4; -.
DR SwissPalm; Q9NQX4; -.
DR BioMuta; MYO5C; -.
DR DMDM; 294862453; -.
DR EPD; Q9NQX4; -.
DR jPOST; Q9NQX4; -.
DR MassIVE; Q9NQX4; -.
DR MaxQB; Q9NQX4; -.
DR PaxDb; Q9NQX4; -.
DR PeptideAtlas; Q9NQX4; -.
DR PRIDE; Q9NQX4; -.
DR ProteomicsDB; 66876; -.
DR ProteomicsDB; 82223; -. [Q9NQX4-1]
DR Antibodypedia; 24945; 65 antibodies from 16 providers.
DR DNASU; 55930; -.
DR Ensembl; ENST00000261839.12; ENSP00000261839.7; ENSG00000128833.13. [Q9NQX4-1]
DR Ensembl; ENST00000559459.5; ENSP00000454064.1; ENSG00000128833.13. [Q9NQX4-2]
DR GeneID; 55930; -.
DR KEGG; hsa:55930; -.
DR MANE-Select; ENST00000261839.12; ENSP00000261839.7; NM_018728.4; NP_061198.2.
DR UCSC; uc010bff.4; human. [Q9NQX4-1]
DR CTD; 55930; -.
DR DisGeNET; 55930; -.
DR GeneCards; MYO5C; -.
DR HGNC; HGNC:7604; MYO5C.
DR HPA; ENSG00000128833; Low tissue specificity.
DR MIM; 610022; gene.
DR neXtProt; NX_Q9NQX4; -.
DR OpenTargets; ENSG00000128833; -.
DR PharmGKB; PA31409; -.
DR VEuPathDB; HostDB:ENSG00000128833; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000157971; -.
DR HOGENOM; CLU_000192_9_4_1; -.
DR InParanoid; Q9NQX4; -.
DR OMA; PDPTEGW; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q9NQX4; -.
DR TreeFam; TF328771; -.
DR PathwayCommons; Q9NQX4; -.
DR SignaLink; Q9NQX4; -.
DR BioGRID-ORCS; 55930; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; MYO5C; human.
DR GenomeRNAi; 55930; -.
DR Pharos; Q9NQX4; Tbio.
DR PRO; PR:Q9NQX4; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NQX4; protein.
DR Bgee; ENSG00000128833; Expressed in bronchial epithelial cell and 186 other tissues.
DR ExpressionAtlas; Q9NQX4; baseline and differential.
DR Genevisible; Q9NQX4; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd15476; Myo5c_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR037991; Myo5c_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Coiled coil; Direct protein sequencing;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..1742
FT /note="Unconventional myosin-Vc"
FT /id="PRO_0000123463"
FT DOMAIN 8..62
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 67..753
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 756..779
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 780..806
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 807..829
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 830..854
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 855..884
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1421..1697
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 632..654
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT COILED 884..1351
FT /evidence="ECO:0000255"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT VAR_SEQ 425..430
FT /note="GKQHTF -> VLKPLM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056592"
FT VAR_SEQ 431..1742
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056593"
FT VARIANT 172
FT /note="R -> C (in dbSNP:rs55686434)"
FT /id="VAR_061365"
FT VARIANT 522
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:11870218"
FT /id="VAR_010646"
FT VARIANT 634
FT /note="L -> S"
FT /id="VAR_010647"
FT VARIANT 1075
FT /note="E -> K (in dbSNP:rs3825801)"
FT /id="VAR_024544"
FT VARIANT 1396
FT /note="P -> L (in dbSNP:rs17650440)"
FT /id="VAR_056186"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:5HMP"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 299..312
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 317..333
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 391..420
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 447..467
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 469..477
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 491..498
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 503..512
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 518..529
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 543..549
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 562..567
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 572..579
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 584..589
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 624..640
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 642..650
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 663..672
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 675..684
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:5HMP"
FT HELIX 693..698
FT /evidence="ECO:0007829|PDB:4ZG4"
FT TURN 706..708
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 714..722
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 728..733
FT /evidence="ECO:0007829|PDB:4ZG4"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 744..751
FT /evidence="ECO:0007829|PDB:4ZG4"
FT HELIX 1371..1378
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1388..1391
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1395..1408
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1413..1433
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1438..1457
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1462..1464
FT /evidence="ECO:0007829|PDB:4L8T"
FT TURN 1470..1474
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1483..1516
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1548..1563
FT /evidence="ECO:0007829|PDB:4L8T"
FT TURN 1564..1566
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1569..1593
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1595..1597
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1600..1619
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1625..1642
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1650..1657
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1663..1672
FT /evidence="ECO:0007829|PDB:4L8T"
FT STRAND 1677..1680
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1685..1694
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1695..1697
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1725..1727
FT /evidence="ECO:0007829|PDB:4L8T"
FT HELIX 1732..1734
FT /evidence="ECO:0007829|PDB:4L8T"
SQ SEQUENCE 1742 AA; 202810 MW; 790B1518098B9054 CRC64;
MAVAELYTQY NRVWIPDPEE VWKSAEIAKD YRVGDKVLRL LLEDGTELDY SVNPESLPPL
RNPDILVGEN DLTALSYLHE PAVLHNLRIR FAESKLIYTY SGIILVAMNP YKQLPIYGDA
IIHAYSGQNM GDMDPHIFAV AEEAYKQMAR NNRNQSIIVS GESGAGKTVS ARYAMRYFAT
VSKSGSNAHV EDKVLASNPI TEAVGNAKTT RNDNSSRFGK YTEISFDEQN QIIGANMSTY
LLEKSRVVFQ SENERNYHIF YQLCASAQQS EFKHLKLGSA EEFNYTRMGG NTVIEGVNDR
AEMVETQKTF TLLGFKEDFQ MDVFKILAAI LHLGNVQITA VGNERSSVSE DDSHLKVFCE
LLGLESGRVA QWLCNRKIVT SSETVVKPMT RPQAVNARDA LAKKIYAHLF DFIVERINQA
LQFSGKQHTF IGVLDIYGFE TFDVNSFEQF CINYANEKLQ QQFNMHVFKL EQEEYMKEDI
PWTLIDFYDN QPVIDLIEAK MGILELLDEE CLLPHGTDEN WLQKLYNNFV NRNPLFEKPR
MSNTSFVIQH FADKVEYKCE GFLEKNRDTV YDMLVEILRA SKFHLCANFF QENPTPPSPF
GSMITVKSAK QVIKPNSKHF RTTVGSKFRS SLYLLMETLN ATTPHYVRCI KPNDEKLPFE
FDSKRIVQQL RACGVLETIR ISAQSYPSRW TYIEFYSRYG ILMTKQELSF SDKKEVCKVV
LHRLIQDSNQ YQFGKTKIFF RAGQVAYLEK LRLDKLRQSC VMVQKHMRGW LQRKKFLRER
RAALIIQQYF RGQQTVRKAI TAVALKEAWA AIIIQKHCRG YLVRSLYQLI RMATITMQAY
SRGFLARRRY RKMLEEHKAV ILQKYARAWL ARRRFQSIRR FVLNIQLTYR VQRLQKKLED
QNKENHGLVE KLTSLAALRA GDVEKIQKLE AELEKAATHR RNYEEKGKRY RDAVEEKLAK
LQKHNSELET QKEQIQLKLQ EKTEELKEKM DNLTKQLFDD VQKEERQRML LEKSFELKTQ
DYEKQIQSLK EEIKALKDEK MQLQHLVEGE HVTSDGLKAE VARLSKQVKT ISEFEKEIEL
LQAQKIDVEK HVQSQKREMR EKMSEITKQL LESYDIEDVR SRLSVEDLEH LNEDGELWFA
YEGLKKATRV LESHFQSQKD CYEKEIEALN FKVVHLSQEI NHLQKLFREE NDINESIRHE
VTRLTSENMM IPDFKQQISE LEKQKQDLEI RLNEQAEKMK GKLEELSNQL HRSQEEEGTQ
RKALEAQNEI HTKEKEKLID KIQEMQEASD HLKKQFETES EVKCNFRQEA SRLTLENRDL
EEELDMKDRV IKKLQDQVKT LSKTIGKAND VHSSSGPKEY LGMLQYKRED EAKLIQNLIL
DLKPRGVVVN MIPGLPAHIL FMCVRYADSL NDANMLKSLM NSTINGIKQV VKEHLEDFEM
LSFWLSNTCH FLNCLKQYSG EEEFMKHNSP QQNKNCLNNF DLSEYRQILS DVAIRIYHQF
IIIMEKNIQP IIVPGMLEYE SLQGISGLKP TGFRKRSSSI DDTDGYTMTS VLQQLSYFYT
TMCQNGLDPE LVRQAVKQLF FLIGAVTLNS LFLRKDMCSC RKGMQIRCNI SYLEEWLKDK
NLQNSLAKET LEPLSQAAWL LQVKKTTDSD AKEIYERCTS LSAVQIIKIL NSYTPIDDFE
KRVTPSFVRK VQALLNSRED SSQLMLDTKY LFQVTFPFTP SPHALEMIQI PSSFKLGFLN
RL
