ABCE1_HUMAN
ID ABCE1_HUMAN Reviewed; 599 AA.
AC P61221; O88793; Q13181; Q13864; Q6NR76; Q96AL0; Q96B10; Q99K66;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=ATP-binding cassette sub-family E member 1;
DE AltName: Full=2'-5'-oligoadenylate-binding protein;
DE AltName: Full=HuHP68;
DE AltName: Full=RNase L inhibitor;
DE AltName: Full=Ribonuclease 4 inhibitor;
DE Short=RNS4I;
GN Name=ABCE1; Synonyms=RLI, RNASEL1, RNASELI, RNS4I; ORFNames=OK/SW-cl.40;
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], CHARACTERIZATION, AND INTERACTION WITH RNASEL.
RX PubMed=7539425; DOI=10.1074/jbc.270.22.13308;
RA Bisbal C., Martinand C., Silhol M., Lebleu B., Salehzada T.;
RT "Cloning and characterization of a RNase L inhibitor. A new component of
RT the interferon-regulated 2-5A pathway.";
RL J. Biol. Chem. 270:13308-13317(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8641422; DOI=10.1016/0014-5793(96)00099-3;
RA Aubry F., Mattei M.-G., Barque J.-P., Galibert F.;
RT "Chromosomal localization and expression pattern of the RNase L inhibitor
RT gene.";
RL FEBS Lett. 381:135-139(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Uterus;
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 [7]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND INDUCTION BY EMCV.
RX PubMed=9660177; DOI=10.1046/j.1432-1327.1998.2540248.x;
RA Martinand C., Salehzada T., Silhol M., Lebleu B., Bisbal C.;
RT "RNase L inhibitor (RLI) antisense constructions block partially the down
RT regulation of the 2-5A/RNase L pathway in encephalomyocarditis-virus-
RT (EMCV)-infected cells.";
RL Eur. J. Biochem. 254:248-255(1998).
RN [8]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND INDUCTION BY HIV-1.
RX PubMed=9847332; DOI=10.1128/jvi.73.1.290-296.1999;
RA Martinand C., Montavon C., Salehzada T., Silhol M., Lebleu B., Bisbal C.;
RT "RNase L inhibitor is induced during human immunodeficiency virus type 1
RT infection and down regulates the 2-5A/RNase L pathway in human T cells.";
RL J. Virol. 73:290-296(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11585831; DOI=10.1074/jbc.m107482200;
RA Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T.;
RT "The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates mitochondrial
RT mRNAs stability in interferon alpha-treated H9 cells.";
RL J. Biol. Chem. 276:48473-48482(2001).
RN [10]
RP INTERACTION WITH HIV-1 VIF AND GAG PROTEINS (MICROBIAL INFECTION).
RX PubMed=11780123; DOI=10.1038/415088a;
RA Zimmerman C., Klein K.C., Kiser P.K., Singh A.R., Firestein B.L.,
RA Riba S.C., Lingappa J.R.;
RT "Identification of a host protein essential for assembly of immature HIV-1
RT capsids.";
RL Nature 415:88-92(2002).
RN [11]
RP INTERACTION WITH HIV-2 PROTEIN GAG (MICROBIAL INFECTION).
RX PubMed=14747530; DOI=10.1128/jvi.78.4.1645-1656.2004;
RA Dooher J.E., Lingappa J.R.;
RT "Conservation of a stepwise, energy-sensitive pathway involving HP68 for
RT assembly of primate lentivirus capsids in cells.";
RL J. Virol. 78:1645-1656(2004).
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 FUNCTION.
RX PubMed=21448132; DOI=10.1038/emboj.2011.93;
RA Pisareva V.P., Skabkin M.A., Hellen C.U., Pestova T.V., Pisarev A.V.;
RT "Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes
RT and stalled elongation complexes.";
RL EMBO J. 30:1804-1817(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND THR-550, 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).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP FUNCTION, INTERACTION WITH PINK1; CNOT4 AND PELO, UBIQUITINATION AT LYS-20,
RP AND MUTAGENESIS OF LYS-20.
RX PubMed=29861391; DOI=10.1016/j.cmet.2018.05.007;
RA Wu Z., Wang Y., Lim J., Liu B., Li Y., Vartak R., Stankiewicz T.,
RA Montgomery S., Lu B.;
RT "Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links
RT Co-translational Quality Control to PINK1-Directed Mitophagy.";
RL Cell Metab. 28:130-144.e7(2018).
RN [17]
RP VARIANT CYS-489, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17488105; DOI=10.1021/pr0700908;
RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA Hendrickson R.C., Stephenson J.L. Jr.;
RT "Detection and validation of non-synonymous coding SNPs from orthogonal
RT analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway (PubMed:21448132). Together with PELO and HBS1L, is
CC required for 48S complex formation from 80S ribosomes and dissociation
CC of vacant 80S ribosomes (PubMed:21448132). Together with PELO and
CC HBS1L, recognizes stalled ribosomes and promotes dissociation of
CC elongation complexes assembled on non-stop mRNAs; this triggers
CC endonucleolytic cleavage of the mRNA, a mechanism to release non-
CC functional ribosomes and to degrade damaged mRNAs as part of the No-Go
CC Decay (NGD) pathway (PubMed:21448132). Plays a role in the regulation
CC of mRNA turnover (By similarity). Plays a role in quality control of
CC translation of mitochondrial outer membrane-localized mRNA
CC (PubMed:29861391). As part of the PINK1-regulated signaling,
CC ubiquitinated by CNOT4 upon mitochondria damage; this modification
CC generates polyubiquitin signals that recruit autophagy receptors to the
CC mitochondrial outer membrane and initiate mitophagy (PubMed:29861391).
CC RNASEL-specific protein inhibitor which antagonizes the binding of 2-5A
CC (5'-phosphorylated 2',5'-linked oligoadenylates) to RNASEL
CC (PubMed:9660177). Negative regulator of the anti-viral effect of the
CC interferon-regulated 2-5A/RNASEL pathway (PubMed:9660177,
CC PubMed:9847332, PubMed:11585831). {ECO:0000250|UniProtKB:P61222,
CC ECO:0000269|PubMed:11585831, ECO:0000269|PubMed:21448132,
CC ECO:0000269|PubMed:29861391, ECO:0000269|PubMed:9660177,
CC ECO:0000269|PubMed:9847332}.
CC -!- FUNCTION: (Microbial infection) May act as a chaperone for post-
CC translational events during HIV-1 capsid assembly.
CC {ECO:0000269|PubMed:9847332}.
CC -!- FUNCTION: (Microbial infection) Plays a role in the down-regulation of
CC the 2-5A/RNASEL pathway during encephalomyocarditis virus (EMCV) and
CC HIV-1 infections. {ECO:0000269|PubMed:9660177}.
CC -!- SUBUNIT: Interacts with PINK1, CNOT4 and PELO (PubMed:29861391).
CC Probably heterodimerizes with RNASEL; this interaction inhibits RNASEL
CC (Probable). {ECO:0000269|PubMed:29861391, ECO:0000305|PubMed:9660177}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 proteins Vif and
CC Gag. {ECO:0000269|PubMed:11780123}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-2 protein Gag.
CC {ECO:0000269|PubMed:14747530}.
CC -!- INTERACTION:
CC P61221; O75822: EIF3J; NbExp=3; IntAct=EBI-2510446, EBI-366647;
CC P61221; P03347-1: gag; Xeno; NbExp=3; IntAct=EBI-2510446, EBI-10687478;
CC P61221; Q9WH76: M; Xeno; NbExp=3; IntAct=EBI-2510446, EBI-10823897;
CC P61221; P69479: P; Xeno; NbExp=3; IntAct=EBI-2510446, EBI-25568013;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11585831}.
CC Mitochondrion {ECO:0000269|PubMed:11585831}. Note=Localized to clusters
CC of virus formation at the plasma membrane.
CC -!- INDUCTION: Activated by encephalomyocarditis virus (EMCV) and HIV-1.
CC {ECO:0000269|PubMed:9660177, ECO:0000269|PubMed:9847332}.
CC -!- PTM: Ubiquitinated by CNOT4 (PubMed:29861391). Ubiquitination mediates
CC the recruitment of autophagy receptors to the mitochondrial outer
CC membrane and initiates mitophagy (PubMed:29861391).
CC {ECO:0000269|PubMed:29861391}.
CC -!- MISCELLANEOUS: The ABC transporter domains seem not to be functional.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/abce1/";
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; X76388; CAA53972.1; -; mRNA.
DR EMBL; X74987; CAA52920.1; -; mRNA.
DR EMBL; AB062293; BAB93476.1; -; mRNA.
DR EMBL; BT009779; AAP88781.1; -; mRNA.
DR EMBL; DQ148409; AAZ38723.1; -; Genomic_DNA.
DR EMBL; BC016283; AAH16283.1; -; mRNA.
DR EMBL; BC016988; AAH16988.1; -; mRNA.
DR CCDS; CCDS34071.1; -.
DR PIR; A57017; A57017.
DR PIR; S63672; S63672.
DR RefSeq; NP_001035809.1; NM_001040876.1.
DR RefSeq; NP_002931.2; NM_002940.2.
DR PDB; 6ZME; EM; 3.00 A; CI=1-599.
DR PDB; 6ZVJ; EM; 3.80 A; 1=4-598.
DR PDB; 7A09; EM; 3.50 A; J=1-599.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; P61221; -.
DR SMR; P61221; -.
DR BioGRID; 111986; 315.
DR IntAct; P61221; 40.
DR MINT; P61221; -.
DR STRING; 9606.ENSP00000296577; -.
DR TCDB; 3.A.1.31.4; the atp-binding cassette (abc) superfamily.
DR CarbonylDB; P61221; -.
DR GlyGen; P61221; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61221; -.
DR MetOSite; P61221; -.
DR PhosphoSitePlus; P61221; -.
DR SwissPalm; P61221; -.
DR BioMuta; ABCE1; -.
DR DMDM; 47117664; -.
DR EPD; P61221; -.
DR jPOST; P61221; -.
DR MassIVE; P61221; -.
DR MaxQB; P61221; -.
DR PaxDb; P61221; -.
DR PeptideAtlas; P61221; -.
DR PRIDE; P61221; -.
DR ProteomicsDB; 57276; -.
DR Antibodypedia; 27438; 328 antibodies from 31 providers.
DR DNASU; 6059; -.
DR Ensembl; ENST00000296577.9; ENSP00000296577.4; ENSG00000164163.11.
DR GeneID; 6059; -.
DR KEGG; hsa:6059; -.
DR MANE-Select; ENST00000296577.9; ENSP00000296577.4; NM_002940.3; NP_002931.2.
DR UCSC; uc003ijy.4; human.
DR CTD; 6059; -.
DR DisGeNET; 6059; -.
DR GeneCards; ABCE1; -.
DR HGNC; HGNC:69; ABCE1.
DR HPA; ENSG00000164163; Low tissue specificity.
DR MIM; 601213; gene.
DR neXtProt; NX_P61221; -.
DR OpenTargets; ENSG00000164163; -.
DR PharmGKB; PA24404; -.
DR VEuPathDB; HostDB:ENSG00000164163; -.
DR eggNOG; KOG0063; Eukaryota.
DR GeneTree; ENSGT00390000015089; -.
DR HOGENOM; CLU_017344_4_1_1; -.
DR InParanoid; P61221; -.
DR OMA; VCVQQAD; -.
DR OrthoDB; 359213at2759; -.
DR PhylomeDB; P61221; -.
DR TreeFam; TF105206; -.
DR PathwayCommons; P61221; -.
DR Reactome; R-HSA-8983711; OAS antiviral response.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; P61221; -.
DR BioGRID-ORCS; 6059; 773 hits in 1058 CRISPR screens.
DR ChiTaRS; ABCE1; human.
DR GenomeRNAi; 6059; -.
DR Pharos; P61221; Tbio.
DR PRO; PR:P61221; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P61221; protein.
DR Bgee; ENSG00000164163; Expressed in adrenal tissue and 199 other tissues.
DR ExpressionAtlas; P61221; baseline and differential.
DR Genevisible; P61221; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IDA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IDA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013283; RLI1.
DR InterPro; IPR034348; RLI_dom_1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR PANTHER; PTHR19248; PTHR19248; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF04068; RLI; 1.
DR PRINTS; PR01868; ABCEFAMILY.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; Chaperone; Cytoplasm;
KW Host-virus interaction; Iron; Iron-sulfur; Isopeptide bond; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Translation regulation; Ubl conjugation.
FT CHAIN 1..599
FT /note="ATP-binding cassette sub-family E member 1"
FT /id="PRO_0000093316"
FT DOMAIN 7..37
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 46..75
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 79..315
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 342..562
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 379..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:29861391"
FT VARIANT 489
FT /note="S -> C (confirmed at protein level;
FT dbSNP:rs3816497)"
FT /evidence="ECO:0000269|PubMed:17488105"
FT /id="VAR_068914"
FT MUTAGEN 20
FT /note="K->R: Abolishes ubiquitination by CNOT4 and
FT diminished the ability to recruit autophagy receptors to
FT damaged mitochondria and to nuclear encoded respiratory
FT chain component mRNA-ribonucleoproteins complexes."
FT /evidence="ECO:0000269|PubMed:29861391"
FT CONFLICT 118
FT /note="T -> A (in Ref. 1; CAA53972)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..179
FT /note="DQIPKA -> ARFLRL (in Ref. 1; CAA53972)"
FT /evidence="ECO:0000305"
FT CONFLICT 471..473
FT /note="ALA -> RLR (in Ref. 1; CAA53972/CAA52920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 67314 MW; 5D582B62E95BC7A6 CRC64;
MADKLTRIAI VNHDKCKPKK CRQECKKSCP VVRMGKLCIE VTPQSKIAWI SETLCIGCGI
CIKKCPFGAL SIVNLPSNLE KETTHRYCAN AFKLHRLPIP RPGEVLGLVG TNGIGKSTAL
KILAGKQKPN LGKYDDPPDW QEILTYFRGS ELQNYFTKIL EDDLKAIIKP QYVDQIPKAA
KGTVGSILDR KDETKTQAIV CQQLDLTHLK ERNVEDLSGG ELQRFACAVV CIQKADIFMF
DEPSSYLDVK QRLKAAITIR SLINPDRYII VVEHDLSVLD YLSDFICCLY GVPSAYGVVT
MPFSVREGIN IFLDGYVPTE NLRFRDASLV FKVAETANEE EVKKMCMYKY PGMKKKMGEF
ELAIVAGEFT DSEIMVMLGE NGTGKTTFIR MLAGRLKPDE GGEVPVLNVS YKPQKISPKS
TGSVRQLLHE KIRDAYTHPQ FVTDVMKPLQ IENIIDQEVQ TLSGGELQRV ALALCLGKPA
DVYLIDEPSA YLDSEQRLMA ARVVKRFILH AKKTAFVVEH DFIMATYLAD RVIVFDGVPS
KNTVANSPQT LLAGMNKFLS QLEITFRRDP NNYRPRINKL NSIKDVEQKK SGNYFFLDD
