AJM1_CAEEL
ID AJM1_CAEEL Reviewed; 1644 AA.
AC A0A1C3NSL9; A0A1C3NSK1; A0A1C3NSK9; A0A1C3NSL1; A0A1C3NSL6; A0A1C3NSM8;
AC A0A1C3NSP2; A0A1C3NSQ2; G4RTG4; H2KYC4; H2KYC6;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Apical junction molecule;
GN Name=ajm-1 {ECO:0000312|WormBase:C25A11.4k};
GN ORFNames=C25A11.4 {ECO:0000312|WormBase:C25A11.4k}, CELE_C25A11.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, AND INTERACTION WITH DLG-1.
RX PubMed=11715019; DOI=10.1038/ncb1101-983;
RA Koeppen M., Simske J.S., Sims P.A., Firestein B.L., Hall D.H., Radice A.D.,
RA Rongo C., Hardin J.D.;
RT "Cooperative regulation of AJM-1 controls junctional integrity in
RT Caenorhabditis elegans epithelia.";
RL Nat. Cell Biol. 3:983-991(2001).
RN [3]
RP INTERACTION WITH DLG-1.
RX PubMed=18411252; DOI=10.1242/jcs.017137;
RA Lockwood C.A., Lynch A.M., Hardin J.;
RT "Dynamic analysis identifies novel roles for DLG-1 subdomains in AJM-1
RT recruitment and LET-413-dependent apical focusing.";
RL J. Cell Sci. 121:1477-1487(2008).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=27623382; DOI=10.1016/j.devcel.2016.07.013;
RA Nechipurenko I.V., Olivier-Mason A., Kazatskaya A., Kennedy J.,
RA McLachlan I.G., Heiman M.G., Blacque O.E., Sengupta P.;
RT "A Conserved role for girdin in basal body positioning and ciliogenesis.";
RL Dev. Cell 38:493-506(2016).
CC -!- FUNCTION: Controls adherens junction integrity (PubMed:11715019).
CC Required for the correct rate and completion of elongation of the
CC embryos (PubMed:11715019). {ECO:0000269|PubMed:11715019}.
CC -!- SUBUNIT: Interacts with dlj-1 (via L27 domain); the interaction
CC regulates ajm-1 apical junction location. {ECO:0000269|PubMed:11715019,
CC ECO:0000269|PubMed:18411252}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}. Cell
CC projection, cilium {ECO:0000269|PubMed:27623382}. Cell junction,
CC adherens junction {ECO:0000269|PubMed:11715019,
CC ECO:0000269|PubMed:27623382}. Note=grdn-1-dependent localization at
CC sensory neuron dendritic tips (PubMed:27623382). The coiled-coil domain
CC is sufficient to localize to apical junctions (PubMed:11715019).
CC {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1;
CC IsoId=A0A1C3NSL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1C3NSL9-2; Sequence=VSP_059285;
CC Name=3;
CC IsoId=A0A1C3NSL9-3; Sequence=VSP_059286;
CC Name=4;
CC IsoId=A0A1C3NSL9-4; Sequence=VSP_059291;
CC Name=5;
CC IsoId=A0A1C3NSL9-5; Sequence=VSP_059292;
CC Name=6;
CC IsoId=A0A1C3NSL9-6; Sequence=VSP_059293;
CC Name=7;
CC IsoId=A0A1C3NSL9-7; Sequence=VSP_059288;
CC Name=8;
CC IsoId=A0A1C3NSL9-8; Sequence=VSP_059293, VSP_059294;
CC Name=9;
CC IsoId=A0A1C3NSL9-9; Sequence=VSP_059290;
CC Name=10;
CC IsoId=A0A1C3NSL9-10; Sequence=VSP_059289;
CC Name=11;
CC IsoId=A0A1C3NSL9-11; Sequence=VSP_059287;
CC -!- TISSUE SPECIFICITY: Expressed by epithelial cells (PubMed:11715019).
CC Expressed in sensory neuron dendritic tips (PubMed:27623382).
CC {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}.
CC -!- DEVELOPMENTAL STAGE: Expression occurs in the embryonic hypodermis,
CC pharynx and intestine, as well as in postembryonic epithelia, including
CC the vulva, uterus, spermathecae, pharynx, intestine, hindgut,
CC hypodermis and male tail. {ECO:0000269|PubMed:11715019}.
CC -!- DOMAIN: The coiled-coil domain is sufficient to localize to apical
CC junctions. {ECO:0000269|PubMed:11715019}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos enclose normally and initiate
CC elongation without obvious morphological abnormalities, yet at a slower
CC rate than the wild type. Elongation is consistently arrested at the 2-
CC 3-fold stage, accompanied by the formation of a large vacuole in the
CC posterior region. {ECO:0000269|PubMed:11715019}.
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DR EMBL; BX284606; SBV53382.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD62273.2; -; Genomic_DNA.
DR EMBL; BX284606; SBV53392.1; -; Genomic_DNA.
DR EMBL; BX284606; SBV53384.1; -; Genomic_DNA.
DR EMBL; BX284606; SBV53383.1; -; Genomic_DNA.
DR EMBL; BX284606; SBV53380.1; -; Genomic_DNA.
DR EMBL; BX284606; SBV53390.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD62272.2; -; Genomic_DNA.
DR EMBL; BX284606; SBV53381.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD62269.1; -; Genomic_DNA.
DR EMBL; BX284606; SBV53391.1; -; Genomic_DNA.
DR RefSeq; NP_001317735.1; NM_001330905.1.
DR RefSeq; NP_001317736.1; NM_001330915.1. [A0A1C3NSL9-2]
DR RefSeq; NP_001317887.1; NM_001330904.1.
DR RefSeq; NP_001317888.1; NM_001330911.1. [A0A1C3NSL9-9]
DR RefSeq; NP_001317889.1; NM_001330908.1. [A0A1C3NSL9-1]
DR RefSeq; NP_001317890.1; NM_001330909.1. [A0A1C3NSL9-5]
DR RefSeq; NP_001317891.1; NM_001330910.1. [A0A1C3NSL9-4]
DR RefSeq; NP_001317897.1; NM_001330912.1. [A0A1C3NSL9-7]
DR RefSeq; NP_001317898.1; NM_001330913.1. [A0A1C3NSL9-11]
DR RefSeq; NP_001317899.1; NM_001330914.1. [A0A1C3NSL9-3]
DR RefSeq; NP_509536.1; NM_077135.1.
DR AlphaFoldDB; A0A1C3NSL9; -.
DR IntAct; A0A1C3NSL9; 6.
DR STRING; 6239.C25A11.4a; -.
DR EnsemblMetazoa; C25A11.4a.1; C25A11.4a.1; WBGene00000100. [A0A1C3NSL9-10]
DR EnsemblMetazoa; C25A11.4a.2; C25A11.4a.2; WBGene00000100. [A0A1C3NSL9-10]
DR EnsemblMetazoa; C25A11.4a.3; C25A11.4a.3; WBGene00000100. [A0A1C3NSL9-10]
DR EnsemblMetazoa; C25A11.4a.4; C25A11.4a.4; WBGene00000100. [A0A1C3NSL9-10]
DR EnsemblMetazoa; C25A11.4d.1; C25A11.4d.1; WBGene00000100. [A0A1C3NSL9-8]
DR EnsemblMetazoa; C25A11.4e.1; C25A11.4e.1; WBGene00000100. [A0A1C3NSL9-2]
DR EnsemblMetazoa; C25A11.4f.1; C25A11.4f.1; WBGene00000100. [A0A1C3NSL9-6]
DR EnsemblMetazoa; C25A11.4g.1; C25A11.4g.1; WBGene00000100. [A0A1C3NSL9-9]
DR EnsemblMetazoa; C25A11.4h.1; C25A11.4h.1; WBGene00000100. [A0A1C3NSL9-7]
DR EnsemblMetazoa; C25A11.4i.1; C25A11.4i.1; WBGene00000100. [A0A1C3NSL9-11]
DR EnsemblMetazoa; C25A11.4j.1; C25A11.4j.1; WBGene00000100. [A0A1C3NSL9-3]
DR EnsemblMetazoa; C25A11.4k.1; C25A11.4k.1; WBGene00000100. [A0A1C3NSL9-1]
DR EnsemblMetazoa; C25A11.4l.1; C25A11.4l.1; WBGene00000100. [A0A1C3NSL9-5]
DR EnsemblMetazoa; C25A11.4m.1; C25A11.4m.1; WBGene00000100. [A0A1C3NSL9-4]
DR GeneID; 181148; -.
DR CTD; 181148; -.
DR WormBase; C25A11.4a; CE27083; WBGene00000100; ajm-1. [A0A1C3NSL9-10]
DR WormBase; C25A11.4d; CE51720; WBGene00000100; ajm-1. [A0A1C3NSL9-8]
DR WormBase; C25A11.4e; CE51736; WBGene00000100; ajm-1. [A0A1C3NSL9-2]
DR WormBase; C25A11.4f; CE51707; WBGene00000100; ajm-1. [A0A1C3NSL9-6]
DR WormBase; C25A11.4g; CE51727; WBGene00000100; ajm-1. [A0A1C3NSL9-9]
DR WormBase; C25A11.4h; CE30251; WBGene00000100; ajm-1. [A0A1C3NSL9-7]
DR WormBase; C25A11.4i; CE51744; WBGene00000100; ajm-1. [A0A1C3NSL9-11]
DR WormBase; C25A11.4j; CE51702; WBGene00000100; ajm-1. [A0A1C3NSL9-3]
DR WormBase; C25A11.4k; CE51717; WBGene00000100; ajm-1. [A0A1C3NSL9-1]
DR WormBase; C25A11.4l; CE51733; WBGene00000100; ajm-1. [A0A1C3NSL9-5]
DR WormBase; C25A11.4m; CE51748; WBGene00000100; ajm-1. [A0A1C3NSL9-4]
DR eggNOG; ENOG502QUPQ; Eukaryota.
DR OMA; YYRREVM; -.
DR OrthoDB; 221103at2759; -.
DR PRO; PR:A0A1C3NSL9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000100; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; A0A1C3NSL9; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0043296; C:apical junction complex; IDA:WormBase.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:WormBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0044292; C:dendrite terminus; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR InterPro; IPR038825; Apical_junction.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR21517; PTHR21517; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Membrane; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1644
FT /note="Apical junction molecule"
FT /id="PRO_0000442928"
FT ZN_FING 1445..1488
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..924
FT /evidence="ECO:0000255"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT VAR_SEQ 1..467
FT /note="Missing (in isoform 2)"
FT /id="VSP_059285"
FT VAR_SEQ 1..368
FT /note="Missing (in isoform 3)"
FT /id="VSP_059286"
FT VAR_SEQ 1..344
FT /note="Missing (in isoform 11)"
FT /id="VSP_059287"
FT VAR_SEQ 1..265
FT /note="Missing (in isoform 7)"
FT /id="VSP_059288"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 10)"
FT /id="VSP_059289"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 9)"
FT /id="VSP_059290"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 4)"
FT /id="VSP_059291"
FT VAR_SEQ 1..96
FT /note="MSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAE
FT SEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHK -> MIPFDPTTSEI
FT HTQKMSQFIV (in isoform 5)"
FT /id="VSP_059292"
FT VAR_SEQ 1
FT /note="M -> MDIENLQSSNNRSQKSRPPDGFNAILQTAFSAILAFVLSLRIIVFAT
FT ARKRLTTTAANPDIQVEEASSSSSDTSSDTEIVEEGVFIQRQGEPTMSEKKPAQGMPSV
FT MSLLQTDEILSSCSDDEPTTSGLIPLPSLIQSNMSVLPNFLHTINEEESDEIRSLTGSS
FT LASPRTVVDRRLSNISLLSPTPDEDFGLEQQEQQPENSEEVRGRESRTSLEEERIVVGE
FT PRTTRQIEITQSASEDDRLDLLKELAKIGKSNTSTSQM (in isoform 6 and
FT isoform 8)"
FT /id="VSP_059293"
FT VAR_SEQ 1088..1128
FT /note="Missing (in isoform 8)"
FT /id="VSP_059294"
SQ SEQUENCE 1644 AA; 193402 MW; F57A629DDA31B700 CRC64;
MSTTTPEKPE EIIDATGTSD TAEKIEVVIS KEEPAEQKNE VEEPDYAQVP AESEDDAAQE
LAPTDSAIQV VHVLEAPQKA ELVTIPLAHS EAEDHKLADA DRDQEEELVF NEERRKTVTM
DDNASLRSAS ITFDANRDEQ DLLNESFASN PTDETVLMQK TKDEMDATSE RPRSPLDLPP
PPASVVLHPS APPPPPPPLS STEVVGNTTT TTTTHYAPKT WNDPSITTAP KIPVSLLSGA
QPLPSVLTQR TTTSSYSAPN YSASSMSGVP SDVAPPPPLP IPNQSSSSAA SYQHHHASSI
SKSISSSRED LLSEHATSRS TVREIPVHRA PSTAPSHSSV FEYHMMPTTT STYHHVETPS
DEYYRREVMT RTIITRSTEA LSQTPLGRPA SPLDRYLPYP TTTTTTSGDG RTREEKTVDY
KVTYHRDIEE QERRIREDQA RRQQEEQDRR DREDNARRIL AQREHQEMER LREQQNLSER
ALAERERADK ERLQQERLLR QQREKKRREE WDRLESIRLA EEEAELARRR ALEKERIDRE
KAEEERKTME RLERERARLE RERLEEERRQ KEKAETERIE RERREHERIE IERIERIKRE
RIERERRERE EKKAEEDRLL RERLELERIE RERRELEARE RQELELQRRE AEDRERQRLE
DEAREMRRRE EERREAELVA DVHRQAEERE RLRKRQEREE AERLERIRLE QQKIDMERID
AERRERERKE EERREFELIE AARRKKEARD RDRLDEMERE RVREEEERRE KERREQERRI
AAEKERKRRQ EEEEEIARLN ELQRAAAARQ AQRNAELDRQ RQRDELDRKA QELSEREMRE
KERRDRERAN EEAQLADLLE RERHNQLIRE NERREAVERA NNRRLEDRRS RDKLDHIVRE
RSEKEQFELE KRRLLAEKEA MNRKKNHLLS SETLAKLTQP MYYTTREPEV TTKVERQVIE
RIDRNVWVED VPYAPSQSAM GYLDNDENNR DRLYNPNDLN RNGSSRSRYQ RAKNEKARRD
FYHSSQDSAD PVTERFRKST DDLTTRSRPE YRGPLLQKFH DSEFRTTALN ETDGLPYRRM
GPSPYEQPFA KLLEETERRY AHYNSRASNP SIYQSSRYYY PERHGQPQHT DNTRAESVVA
YERESRRESP ADQAHIRSRS ADYLMDRRIR EETEVPENQL QKTRVEPHDQ SPRESRISEY
EMRFRKSTEK LTVPDWYREN RPQGQTAQTS TYRYGNGVEP MSTTTTTTTV INGTSSHQQA
PPPVPPQPIG NIGLPRGMFD RYKDDIEELR RSRSSLHQTG QQETSNRQGS TLSVGGIVDQ
GHALPGYTVS EVPNAWNLHT SRTSRVVEVA DTFVGTSSHE YGNFTNRYGG RVTIEEVLDS
IFQKVTPTNQ RLNFDRSYPQ ADELFQGNVD GPGIYTNNYS VMRQVLKSPE RAEHILQNEE
LFVRCTECHR TRELSAARLF FVSCKHCYTY YCSRECRHNN WPNHSGRCSF ARINTLCKDV
IMKVREDEQA QAFMSKVARD GFSVSGRGSV NIRLSSPQLA QAYVSNGWRA LSAYPNDQLL
YYYTVKALIA ERKEPSLIAL CNRYEPREKF ILSVSIIADI EHCPETPPPE TRELSAVQFS
SPRSRYEAIQ NQNAPYFSEF AHNV
