NPL4_YEAST
ID NPL4_YEAST Reviewed; 580 AA.
AC P33755; D6VQG6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nuclear protein localization protein 4;
DE AltName: Full=HMG-CoA reductase degradation protein 4;
GN Name=NPL4; Synonyms=HRD4; OrderedLocusNames=YBR170C; ORFNames=YBR1231;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8930904; DOI=10.1091/mbc.7.11.1835;
RA DeHoratius C., Silver P.A.;
RT "Nuclear transport defects and nuclear envelope alterations are associated
RT with mutation of the Saccharomyces cerevisiae NPL4 gene.";
RL Mol. Biol. Cell 7:1835-1855(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8212898; DOI=10.1002/yea.320090811;
RA Schaaff-Gerstenschlaeger I., Bauer A., Boles E., Zimmermann F.K.;
RT "Sequence and function analysis of a 4.3 kb fragment of Saccharomyces
RT cerevisiae chromosome II including three open reading frames.";
RL Yeast 9:915-921(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, INTERACTION WITH CDC48 AND UFD1, AND SUBCELLULAR LOCATION.
RX PubMed=11733065; DOI=10.1016/s0092-8674(01)00595-5;
RA Rape M., Hoppe T., Gorr I., Kalocay M., Richly H., Jentsch S.;
RT "Mobilization of processed, membrane-tethered SPT23 transcription factor by
RT CDC48(UFD1/NPL4), a ubiquitin-selective chaperone.";
RL Cell 107:667-677(2001).
RN [6]
RP FUNCTION, INTERACTION WITH CDC48 AND UFD1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-323.
RX PubMed=11598205; DOI=10.1091/mbc.12.10.3226;
RA Hitchcock A.L., Krebber H., Frietze S., Lin A., Latterich M., Silver P.A.;
RT "The conserved npl4 protein complex mediates proteasome-dependent membrane-
RT bound transcription factor activation.";
RL Mol. Biol. Cell 12:3226-3241(2001).
RN [7]
RP FUNCTION, INTERACTION WITH CDC48 AND UFD1, AND SUBCELLULAR LOCATION.
RX PubMed=11739805; DOI=10.1091/mbc.12.12.4114;
RA Bays N.W., Wilhovsky S.K., Goradia A., Hodgkiss-Harlow K., Hampton R.Y.;
RT "HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER
RT proteins.";
RL Mol. Biol. Cell 12:4114-4128(2001).
RN [8]
RP FUNCTION.
RX PubMed=11740563; DOI=10.1038/414652a;
RA Ye Y., Meyer H.H., Rapoport T.A.;
RT "The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER
RT into the cytosol.";
RL Nature 414:652-656(2001).
RN [9]
RP FUNCTION.
RX PubMed=11847109; DOI=10.1093/emboj/21.4.615;
RA Braun S., Matuschewski K., Rape M., Thoms S., Jentsch S.;
RT "Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in
RT ERAD of OLE1 and other substrates.";
RL EMBO J. 21:615-621(2002).
RN [10]
RP FUNCTION.
RX PubMed=14636562; DOI=10.1016/s0092-8674(03)00815-8;
RA Cao K., Nakajima R., Meyer H.H., Zheng Y.;
RT "The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of
RT mitosis.";
RL Cell 115:355-367(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP IDENTIFICATION IN CDC48-NPL4-UFD1 ATPASE COMPLEX, AND INTERACTION WITH HRD1
RP COMPLEX.
RX PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
RA Carvalho P., Goder V., Rapoport T.A.;
RT "Distinct ubiquitin-ligase complexes define convergent pathways for the
RT degradation of ER proteins.";
RL Cell 126:361-373(2006).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH DOA1; UFD1; CDC48; OTU1 AND SHP1.
RX PubMed=16427015; DOI=10.1016/j.molcel.2005.12.014;
RA Rumpf S., Jentsch S.;
RT "Functional division of substrate processing cofactors of the ubiquitin-
RT selective Cdc48 chaperone.";
RL Mol. Cell 21:261-269(2006).
RN [14]
RP FUNCTION, AND INTERACTION WITH VMS1.
RX PubMed=21070972; DOI=10.1016/j.molcel.2010.10.021;
RA Heo J.M., Livnat-Levanon N., Taylor E.B., Jones K.T., Dephoure N., Ring J.,
RA Xie J., Brodsky J.L., Madeo F., Gygi S.P., Ashrafi K., Glickman M.H.,
RA Rutter J.;
RT "A stress-responsive system for mitochondrial protein degradation.";
RL Mol. Cell 40:465-480(2010).
RN [15] {ECO:0007744|PDB:6OA9, ECO:0007744|PDB:6OAA}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH CDC48 AND
RP POLYUBIQUITINATED SUBSTRATE, AND FUNCTION.
RX PubMed=31249135; DOI=10.1126/science.aax1033;
RA Twomey E.C., Ji Z., Wales T.E., Bodnar N.O., Ficarro S.B., Marto J.A.,
RA Engen J.R., Rapoport T.A.;
RT "Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin
RT unfolding.";
RL Science 365:0-0(2019).
CC -!- FUNCTION: Substrate-recruiting cofactor of the CDC48-NPL4-UFD1
CC segregase (PubMed:31249135). Assists CDC48 in the dislocation of
CC misfolded, polyubiquitinated ERAD substrates that are subsequently
CC delivered to the proteasome for degradation (PubMed:11739805,
CC PubMed:11740563, PubMed:11847109). Involved in the import of nuclear-
CC targeted proteins into the nucleus and the export of poly(A) RNA out of
CC the nucleus (PubMed:8930904, PubMed:11733065). Required for the
CC proteasome-dependent processing/activation of MGA2 and SPT23
CC transcription factors leading to the subsequent expression of OLE1
CC (PubMed:11733065). Regulates ubiquitin-mediated mitochondria protein
CC degradation (PubMed:31249135). Involved in spindle disassembly probably
CC by promoting the degradation of spindle assemby factors ASE1 and CDC5
CC at the end of mitosis (PubMed:14636562). {ECO:0000269|PubMed:11733065,
CC ECO:0000269|PubMed:11739805, ECO:0000269|PubMed:11740563,
CC ECO:0000269|PubMed:11847109, ECO:0000269|PubMed:14636562,
CC ECO:0000269|PubMed:31249135, ECO:0000269|PubMed:8930904}.
CC -!- SUBUNIT: Component of the heterotrimeric CDC48-NPL4-UFD1 ATPase complex
CC (PubMed:16873066). The CDC48-NPL4-UFD1 ATPase complex interacts with
CC the HRD1 ubiquitin ligase complex composed of the E3 ligase HRD1, its
CC cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and
CC CDC48-binding protein UBX2 (PubMed:16873066). Interaction between the
CC complexes is mediated by interaction between CDC48-NPL4-UFD1 complex
CC member CDC48 and HRD1 complex member UBX2 (PubMed:16873066). Forms a
CC complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and deubiquitinase
CC OTU1 (PubMed:16427015). Interacts with CDC48, UFD1 and VMS1
CC (PubMed:11598205, PubMed:11733065, PubMed:11739805, PubMed:21070972,
CC PubMed:31249135). {ECO:0000269|PubMed:11598205,
CC ECO:0000269|PubMed:11733065, ECO:0000269|PubMed:11739805,
CC ECO:0000269|PubMed:16427015, ECO:0000269|PubMed:16873066,
CC ECO:0000269|PubMed:21070972, ECO:0000269|PubMed:31249135}.
CC -!- INTERACTION:
CC P33755; P25694: CDC48; NbExp=11; IntAct=EBI-12193, EBI-4308;
CC P33755; P53044: UFD1; NbExp=11; IntAct=EBI-12193, EBI-19997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endoplasmic
CC reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
CC Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Localizes mainly at the nuclear periphery and the endoplasmic
CC reticulum membrane.
CC -!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NPL4 family. {ECO:0000305}.
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DR EMBL; X72224; CAA51026.1; -; Genomic_DNA.
DR EMBL; X74437; CAA52450.1; -; Genomic_DNA.
DR EMBL; Z36039; CAA85131.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07286.1; -; Genomic_DNA.
DR PIR; S34340; S34340.
DR RefSeq; NP_009729.1; NM_001178518.1.
DR PDB; 6JWH; X-ray; 1.72 A; A=113-580.
DR PDB; 6JWI; X-ray; 2.55 A; A/E=113-580.
DR PDB; 6JWJ; X-ray; 1.58 A; A=113-580.
DR PDB; 6OA9; EM; 3.90 A; G=1-580.
DR PDB; 6OAA; EM; 4.10 A; G=1-580.
DR PDBsum; 6JWH; -.
DR PDBsum; 6JWI; -.
DR PDBsum; 6JWJ; -.
DR PDBsum; 6OA9; -.
DR PDBsum; 6OAA; -.
DR AlphaFoldDB; P33755; -.
DR SMR; P33755; -.
DR BioGRID; 32870; 268.
DR ComplexPortal; CPX-2946; CDC48-NPL4-UFD1 AAA ATPase complex.
DR ComplexPortal; CPX-3069; CDC48-NPL4-VMS1 AAA ATPase complex.
DR ComplexPortal; CPX-3265; Ribosome quality control complex.
DR DIP; DIP-1475N; -.
DR IntAct; P33755; 18.
DR MINT; P33755; -.
DR STRING; 4932.YBR170C; -.
DR TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; P33755; -.
DR MaxQB; P33755; -.
DR PaxDb; P33755; -.
DR PRIDE; P33755; -.
DR EnsemblFungi; YBR170C_mRNA; YBR170C; YBR170C.
DR GeneID; 852468; -.
DR KEGG; sce:YBR170C; -.
DR SGD; S000000374; NPL4.
DR VEuPathDB; FungiDB:YBR170C; -.
DR eggNOG; KOG2834; Eukaryota.
DR GeneTree; ENSGT00390000018731; -.
DR HOGENOM; CLU_017172_0_0_1; -.
DR InParanoid; P33755; -.
DR OMA; KWSRTGR; -.
DR BioCyc; YEAST:G3O-29118-MON; -.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:P33755; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P33755; protein.
DR GO; GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030894; C:replisome; IDA:SGD.
DR GO; GO:1990112; C:RQC complex; IDA:SGD.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:SGD.
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:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR GO; GO:0006274; P:DNA replication termination; IDA:SGD.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0051228; P:mitotic spindle disassembly; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IMP:SGD.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0072665; P:protein localization to vacuole; IMP:SGD.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IC:ComplexPortal.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:SGD.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd08061; MPN_NPL4; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR016563; Npl4.
DR InterPro; IPR007717; NPL4_C.
DR InterPro; IPR007716; NPL4_Zn-bd_put.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12710; PTHR12710; 1.
DR Pfam; PF05021; NPL4; 1.
DR Pfam; PF05020; zf-NPL4; 1.
DR PIRSF; PIRSF010052; Polyub_prc_Npl4; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Membrane; mRNA transport;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..580
FT /note="Nuclear protein localization protein 4"
FT /id="PRO_0000057944"
FT DOMAIN 237..377
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MUTAGEN 323
FT /note="G->S: In npl4-1; nuclear-targeted proteins
FT accumulate in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:11598205"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6JWI"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6JWJ"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:6JWI"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 260..270
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 300..316
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 352..364
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:6JWH"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:6JWJ"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6JWI"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 501..512
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 517..524
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 527..535
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 541..552
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 557..565
FT /evidence="ECO:0007829|PDB:6JWJ"
FT HELIX 567..577
FT /evidence="ECO:0007829|PDB:6JWJ"
SQ SEQUENCE 580 AA; 65782 MW; 6EF35D21338EE07E CRC64;
MLIRFRSKNG THRVSCQEND LFGTVIEKLV GNLDPNADVD TFTVCEKPGQ GIHAVSELAD
RTVMDLGLKH GDMLILNYSD KPANEKDGVN VEIGSVGIDS KGIRQHRYGP LRIKELAVDE
ELEKEDGLIP RQKSKLCKHG DRGMCEYCSP LPPWDKEYHE KNKIKHISFH SYLKKLNENA
NKKENGSSYI SPLSEPDFRI NKRCHNGHEP WPRGICSKCQ PSAITLQQQE FRMVDHVEFQ
KSEIINEFIQ AWRYTGMQRF GYMYGSYSKY DNTPLGIKAV VEAIYEPPQH DEQDGLTMDV
EQVKNEMLQI DRQAQEMGLS RIGLIFTDLS DAGAGDGSVF CKRHKDSFFL SSLEVIMAAR
HQTRHPNVSK YSEQGFFSSK FVTCVISGNL EGEIDISSYQ VSTEAEALVT ADMISGSTFP
SMAYINDTTD ERYVPEIFYM KSNEYGITVK ENAKPAFPVD YLLVTLTHGF PNTDTETNSK
FVSSTGFPWS NRQAMGQSQD YQELKKYLFN VASSGDFNLL HEKISNFHLL LYINSLQILS
PDEWKLLIES AVKNEWEESL LKLVSSAGWQ TLVMILQESG
