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Database: UniProt
Entry: P33755
LinkDB: P33755
Original site: P33755 
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   29-SEP-2021, entry version 164.
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   SMR; P33755; -.
DR   BioGRID; 32870; 264.
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; PQQFRMV; -.
DR   Reactome; R-SCE-110320; Translesion Synthesis by POLH.
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; IMP:SGD.
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: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; IMP:SGD.
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   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
//
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