NPL4_HUMAN
ID NPL4_HUMAN Reviewed; 608 AA.
AC Q8TAT6; Q8N3J1; Q9H8V2; Q9H964; Q9NWR5; Q9P229;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Nuclear protein localization protein 4 homolog;
DE Short=Protein NPL4;
GN Name=NPLOC4; Synonyms=KIAA1499, NPL4;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 MRNA].
RC TISSUE=Pancreas;
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 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-608.
RC TISSUE=Melanoma;
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 [6]
RP INTERACTION WITH UFD1, AND TISSUE SPECIFICITY.
RX PubMed=11574150; DOI=10.1016/s0378-1119(01)00649-7;
RA Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B., Novelli G.;
RT "Cloning and characterization of the gene encoding human NPL4, a protein
RT interacting with the ubiquitin fusion-degradation protein (UFD1L).";
RL Gene 275:39-46(2001).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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 [9]
RP INTERACTION WITH ZFAND2B.
RX PubMed=24160817; DOI=10.1042/bj20130710;
RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA Edelmann M.J., Kessler B.M., Stanhill A.;
RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT complex.";
RL Biochem. J. 457:253-261(2014).
RN [10]
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 [11]
RP FUNCTION, INTERACTION WITH UFD1 AND VCP, AND MUTAGENESIS OF 6-ILE--ARG-8;
RP ARG-17 AND ARG-50.
RX PubMed=26471729; DOI=10.15252/embj.201591888;
RA Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
RA Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
RT "A non-canonical role of the p97 complex in RIG-I antiviral signaling.";
RL EMBO J. 34:2903-2920(2015).
CC -!- FUNCTION: The ternary complex containing UFD1, VCP and NPLOC4 binds
CC ubiquitinated proteins and is necessary for the export of misfolded
CC proteins from the ER to the cytoplasm, where they are degraded by the
CC proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly
CC at the end of mitosis and is necessary for the formation of a closed
CC nuclear envelope (By similarity). Acts as a negative regulator of type
CC I interferon production via the complex formed with VCP and UFD1, which
CC binds to DDX58/RIG-I and recruits RNF125 to promote ubiquitination and
CC degradation of DDX58/RIG-I (PubMed:26471729).
CC {ECO:0000250|UniProtKB:Q9ES54, ECO:0000269|PubMed:26471729}.
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC -!- SUBUNIT: Heterodimer with UFD1 (PubMed:11574150, PubMed:26471729). The
CC heterodimer binds ubiquitinated proteins (By similarity). The
CC heterodimer binds to VCP and inhibits Golgi membrane fusion
CC (PubMed:11574150, PubMed:26471729). Interacts with ZFAND2B; probably
CC through VCP (PubMed:24160817). {ECO:0000250|UniProtKB:Q9ES54,
CC ECO:0000269|PubMed:11574150, ECO:0000269|PubMed:24160817,
CC ECO:0000269|PubMed:26471729}.
CC -!- INTERACTION:
CC Q8TAT6; P37173: TGFBR2; NbExp=3; IntAct=EBI-1994109, EBI-296151;
CC Q8TAT6; Q92890: UFD1; NbExp=8; IntAct=EBI-1994109, EBI-1994090;
CC Q8TAT6; P55072: VCP; NbExp=9; IntAct=EBI-1994109, EBI-355164;
CC Q8TAT6; Q4G0F5: VPS26B; NbExp=3; IntAct=EBI-1994109, EBI-6151831;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9ES54}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9ES54}. Nucleus {ECO:0000250|UniProtKB:Q9ES54}.
CC Note=Associated with the endoplasmic reticulum and nuclear.
CC {ECO:0000250|UniProtKB:Q9ES54}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TAT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAT6-2; Sequence=VSP_009789;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, heart,
CC skeletal muscle, kidney and fetal liver. {ECO:0000269|PubMed:11574150}.
CC -!- DOMAIN: Binds ubiquitinated proteins via its RanBP2-type zinc finger.
CC {ECO:0000250|UniProtKB:Q9ES54}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NPL4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91314.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA96023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14372.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB040932; BAA96023.1; ALT_INIT; mRNA.
DR EMBL; AK000664; BAA91314.1; ALT_INIT; mRNA.
DR EMBL; AK023046; BAB14372.1; ALT_INIT; mRNA.
DR EMBL; AK023272; BAB14499.1; ALT_INIT; mRNA.
DR EMBL; BC025930; AAH25930.1; -; mRNA.
DR EMBL; AL834300; CAD38971.1; -; mRNA.
DR CCDS; CCDS45812.1; -. [Q8TAT6-1]
DR RefSeq; NP_060391.2; NM_017921.3. [Q8TAT6-1]
DR RefSeq; XP_011523281.1; XM_011524979.1. [Q8TAT6-2]
DR AlphaFoldDB; Q8TAT6; -.
DR SMR; Q8TAT6; -.
DR BioGRID; 120798; 195.
DR ComplexPortal; CPX-137; VCP-NPL4-UFD1 AAA ATPase complex.
DR CORUM; Q8TAT6; -.
DR DIP; DIP-44059N; -.
DR IntAct; Q8TAT6; 42.
DR MINT; Q8TAT6; -.
DR STRING; 9606.ENSP00000331487; -.
DR TCDB; 3.A.16.1.1; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; Q8TAT6; -.
DR PhosphoSitePlus; Q8TAT6; -.
DR SwissPalm; Q8TAT6; -.
DR BioMuta; NPLOC4; -.
DR DMDM; 50428974; -.
DR EPD; Q8TAT6; -.
DR jPOST; Q8TAT6; -.
DR MassIVE; Q8TAT6; -.
DR MaxQB; Q8TAT6; -.
DR PaxDb; Q8TAT6; -.
DR PeptideAtlas; Q8TAT6; -.
DR PRIDE; Q8TAT6; -.
DR ProteomicsDB; 73917; -. [Q8TAT6-1]
DR ProteomicsDB; 73918; -. [Q8TAT6-2]
DR Antibodypedia; 10070; 144 antibodies from 28 providers.
DR DNASU; 55666; -.
DR Ensembl; ENST00000331134.11; ENSP00000331487.5; ENSG00000182446.14. [Q8TAT6-1]
DR Ensembl; ENST00000374747.9; ENSP00000363879.5; ENSG00000182446.14. [Q8TAT6-2]
DR GeneID; 55666; -.
DR KEGG; hsa:55666; -.
DR MANE-Select; ENST00000331134.11; ENSP00000331487.5; NM_017921.4; NP_060391.2.
DR UCSC; uc002kat.5; human. [Q8TAT6-1]
DR CTD; 55666; -.
DR DisGeNET; 55666; -.
DR GeneCards; NPLOC4; -.
DR HGNC; HGNC:18261; NPLOC4.
DR HPA; ENSG00000182446; Tissue enhanced (skeletal).
DR MIM; 606590; gene.
DR neXtProt; NX_Q8TAT6; -.
DR OpenTargets; ENSG00000182446; -.
DR PharmGKB; PA143485558; -.
DR VEuPathDB; HostDB:ENSG00000182446; -.
DR eggNOG; KOG2834; Eukaryota.
DR GeneTree; ENSGT00390000018731; -.
DR HOGENOM; CLU_017172_2_0_1; -.
DR InParanoid; Q8TAT6; -.
DR OMA; KWSRTGR; -.
DR OrthoDB; 1106766at2759; -.
DR PhylomeDB; Q8TAT6; -.
DR TreeFam; TF314173; -.
DR PathwayCommons; Q8TAT6; -.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR SignaLink; Q8TAT6; -.
DR SIGNOR; Q8TAT6; -.
DR UniPathway; UPA00144; -.
DR BioGRID-ORCS; 55666; 776 hits in 1080 CRISPR screens.
DR ChiTaRS; NPLOC4; human.
DR GeneWiki; NPLOC4; -.
DR GenomeRNAi; 55666; -.
DR Pharos; Q8TAT6; Tbio.
DR PRO; PR:Q8TAT6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8TAT6; protein.
DR Bgee; ENSG00000182446; Expressed in gastrocnemius and 194 other tissues.
DR ExpressionAtlas; Q8TAT6; baseline and differential.
DR Genevisible; Q8TAT6; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; ISS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0036501; C:UFD1-NPL4 complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:HGNC-UCL.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IMP:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IMP:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:HGNC-UCL.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR CDD; cd08061; MPN_NPL4; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR016563; Npl4.
DR InterPro; IPR007717; NPL4_C.
DR InterPro; IPR024682; Npl4_Ub-like_dom.
DR InterPro; IPR007716; NPL4_Zn-bd_put.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR12710; PTHR12710; 1.
DR Pfam; PF05021; NPL4; 1.
DR Pfam; PF11543; UN_NPL4; 1.
DR Pfam; PF05020; zf-NPL4; 1.
DR PIRSF; PIRSF010052; Polyub_prc_Npl4; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Metal-binding; Nucleus;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..608
FT /note="Nuclear protein localization protein 4 homolog"
FT /id="PRO_0000057941"
FT DOMAIN 226..363
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT ZN_FING 580..608
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60670"
FT VAR_SEQ 558..608
FT /note="TVGGQLPGLHEYGAVGGSTHTATAAMWACQHCTFMNQPGTGHCEMCSLPRT
FT -> EYPHPLPRHPVAGAGEQPTLHSSPLPVVPWIPHPAASWQVPSAMQRVETRPPCQAR
FT GRLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_009789"
FT MUTAGEN 6..8
FT /note="IIR->AIA: Abolished interaction with VCP; when
FT associated with A-17 and A-50."
FT /evidence="ECO:0000269|PubMed:26471729"
FT MUTAGEN 17
FT /note="R->A: Abolished interaction with VCP; when
FT associated with 6-A--A-8 and A-50."
FT /evidence="ECO:0000269|PubMed:26471729"
FT MUTAGEN 50
FT /note="R->A: Abolished interaction with VCP; when
FT associated with 6-A--A-8 and A-17."
FT /evidence="ECO:0000269|PubMed:26471729"
FT CONFLICT 246
FT /note="N -> S (in Ref. 2; BAB14499)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="H -> Q (in Ref. 2; BAA91314)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="G -> E (in Ref. 2; BAA91314)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="M -> V (in Ref. 2; BAB14499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 68120 MW; 6ED6A0145F15C01D CRC64;
MAESIIIRVQ SPDGVKRITA TKRETAATFL KKVAKEFGFQ NNGFSVYINR NKTGEITASS
NKSLNLLKIK HGDLLFLFPS SLAGPSSEME TSVPPGFKVF GAPNVVEDEI DQYLSKQDGK
IYRSRDPQLC RHGPLGKCVH CVPLEPFDED YLNHLEPPVK HMSFHAYIRK LTGGADKGKF
VALENISCKI KSGCEGHLPW PNGICTKCQP SAITLNRQKY RHVDNIMFEN HTVADRFLDF
WRKTGNQHFG YLYGRYTEHK DIPLGIRAEV AAIYEPPQIG TQNSLELLED PKAEVVDEIA
AKLGLRKVGW IFTDLVSEDT RKGTVRYSRN KDTYFLSSEE CITAGDFQNK HPNMCRLSPD
GHFGSKFVTA VATGGPDNQV HFEGYQVSNQ CMALVRDECL LPCKDAPELG YAKESSSEQY
VPDVFYKDVD KFGNEITQLA RPLPVEYLII DITTTFPKDP VYTFSISQNP FPIENRDVLG
ETQDFHSLAT YLSQNTSSVF LDTISDFHLL LFLVTNEVMP LQDSISLLLE AVRTRNEELA
QTWKRSEQWA TIEQLCSTVG GQLPGLHEYG AVGGSTHTAT AAMWACQHCT FMNQPGTGHC
EMCSLPRT
