GenomeNet

Database: UniProt
Entry: P0CG63
LinkDB: P0CG63
Original site: P0CG63 
ID   UBI4P_YEAST             Reviewed;         381 AA.
AC   P0CG63; D6VXW7; P04838; P61864; Q6LA96;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   29-SEP-2021, entry version 99.
DE   RecName: Full=Polyubiquitin {ECO:0000303|PubMed:3038523};
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Flags: Precursor;
GN   Name=UBI4 {ECO:0000303|PubMed:3038523}; Synonyms=SCD2;
GN   OrderedLocusNames=YLL039C {ECO:0000312|SGD:S000003962};
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].
RX   PubMed=3038523; DOI=10.1002/j.1460-2075.1987.tb02384.x;
RA   Oezkaynak E., Finley D., Solomon M.J., Varshavsky A.;
RT   "The yeast ubiquitin genes: a family of natural gene fusions.";
RL   EMBO J. 6:1429-1439(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-381.
RX   PubMed=6095120; DOI=10.1038/312663a0;
RA   Oezkaynak E., Finley D., Varshavsky A.;
RT   "The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin
RT   precursor protein.";
RL   Nature 312:663-666(1984).
RN   [5]
RP   MUTAGENESIS OF LYS-29; LYS-48 AND LYS-63.
RX   PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
RA   Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
RT   "A proteolytic pathway that recognizes ubiquitin as a degradation signal.";
RL   J. Biol. Chem. 270:17442-17456(1995).
RN   [6]
RP   MUTAGENESIS OF LYSINE RESIDUES.
RX   PubMed=7862120; DOI=10.1128/mcb.15.3.1265;
RA   Spence J., Sadis S., Haas A.L., Finley D.;
RT   "A ubiquitin mutant with specific defects in DNA repair and
RT   multiubiquitination.";
RL   Mol. Cell. Biol. 15:1265-1273(1995).
RN   [7]
RP   UBIQUITINATION AT LYS-48 AND GLY-76.
RX   PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA   Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA   Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA   Inada T.;
RT   "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT   control.";
RL   Nat. Commun. 8:159-159(2017).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH YUH1.
RX   PubMed=10406793; DOI=10.1093/emboj/18.14.3877;
RA   Johnston S.C., Riddle S.M., Cohen R.E., Hill C.P.;
RT   "Structural basis for the specificity of ubiquitin C-terminal hydrolases.";
RL   EMBO J. 18:3877-3887(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH VPS9.
RX   PubMed=12628920; DOI=10.1093/emboj/cdg140;
RA   Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L.;
RT   "A ubiquitin-binding motif required for intramolecular monoubiquitylation,
RT   the CUE domain.";
RL   EMBO J. 22:1273-1281(2003).
RN   [10]
RP   STRUCTURE BY NMR IN COMPLEX WITH UBC1.
RX   PubMed=11591345; DOI=10.1016/s0969-2126(01)00657-8;
RA   Hamilton K.S., Ellison M.J., Barber K.R., Williams R.S., Huzil J.T.,
RA   McKenna S., Ptak C., Glover M., Shaw G.S.;
RT   "Structure of a conjugating enzyme-ubiquitin thiolester intermediate
RT   reveals a novel role for the ubiquitin tail.";
RL   Structure 9:897-904(2001).
RN   [11]
RP   STRUCTURE BY NMR OF COMPLEX WITH CUE2 N-TERMINAL DOMAIN.
RX   PubMed=12787503; DOI=10.1016/s0092-8674(03)00362-3;
RA   Kang R.S., Daniels C.M., Francis S.A., Shih S.C., Salerno W.J., Hicke L.,
RA   Radhakrishnan I.;
RT   "Solution structure of a CUE-ubiquitin complex reveals a conserved mode of
RT   ubiquitin binding.";
RL   Cell 113:621-630(2003).
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is conjugated
CC       to target proteins via an isopeptide bond either as a monomer
CC       (monoubiquitin), a polymer linked via different Lys residues of the
CC       ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC       initiator Met of the ubiquitin (linear polyubiquitin chains).
CC       Polyubiquitin chains, when attached to a target protein, have different
CC       functions depending on the Lys residue of the ubiquitin that is linked:
CC       Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC       cycle regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked is
CC       involved in endocytosis, and DNA-damage responses. Linear polymer
CC       chains formed via attachment by the initiator Met lead to cell
CC       signaling. Ubiquitin is usually conjugated to Lys residues of target
CC       proteins, however, in rare cases, conjugation to Cys or Ser residues
CC       has been observed. When polyubiquitin is free (unanchored-
CC       polyubiquitin), it also has distinct roles, such as in activation of
CC       protein kinases, and in signaling (By similarity).
CC       {ECO:0000250|UniProtKB:P0CG47}.
CC   -!- INTERACTION:
CC       P0CG63; P40087: DDI1; NbExp=3; IntAct=EBI-7000452, EBI-5717;
CC       P0CG63; P48510: DSK2; NbExp=3; IntAct=EBI-7000452, EBI-6174;
CC       P0CG63; P48365: GYP7; NbExp=2; IntAct=EBI-7000452, EBI-8018;
CC       P0CG63; P32628: RAD23; NbExp=4; IntAct=EBI-7000452, EBI-14668;
CC       P0CG63; P00358: TDH2; NbExp=2; IntAct=EBI-7000452, EBI-7212;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250|UniProtKB:Q15843}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBI1 and UBI2
CC       genes code for a single copy of ubiquitin fused to the ribosomal
CC       proteins L40. UBI3 is a polyprotein with one copy of ubiquitin fused to
CC       ribosomal protein S37. UBI4 is a polyprotein containing 5 exact head to
CC       tail repeats of ubiquitin.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR   EMBL; X05731; CAA29198.1; -; Genomic_DNA.
DR   EMBL; Z73144; CAA97489.1; -; Genomic_DNA.
DR   EMBL; X01473; CAA25704.1; -; Genomic_DNA.
DR   EMBL; X01474; CAA25706.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09283.1; -; Genomic_DNA.
DR   PIR; D29456; UQBY.
DR   RefSeq; NP_013061.1; NM_001181859.1.
DR   PDB; 1OTR; NMR; -; B=1-76.
DR   PDB; 1Q0W; NMR; -; B=1-76.
DR   PDB; 1WR1; NMR; -; A=1-76.
DR   PDB; 1ZW7; NMR; -; A=1-76.
DR   PDB; 2G3Q; NMR; -; B=1-76.
DR   PDB; 2JT4; NMR; -; B=1-76.
DR   PDB; 2JWZ; NMR; -; A=1-76.
DR   PDB; 2KDI; NMR; -; A=2-76.
DR   PDB; 2L00; NMR; -; B=1-76.
DR   PDB; 3CMM; X-ray; 2.70 A; B/D=1-76.
DR   PDB; 3L0W; X-ray; 2.80 A; B=1-76.
DR   PDB; 3L10; X-ray; 2.80 A; B=1-76.
DR   PDB; 3OLM; X-ray; 2.50 A; D=1-76.
DR   PDB; 4HCN; X-ray; 2.60 A; B=1-76.
DR   PDB; 4NNJ; X-ray; 2.40 A; B/D/E=305-380.
DR   PDB; 4Q5E; X-ray; 1.87 A; B=305-380.
DR   PDB; 4Q5H; X-ray; 2.00 A; B=305-380.
DR   PDBsum; 1OTR; -.
DR   PDBsum; 1Q0W; -.
DR   PDBsum; 1WR1; -.
DR   PDBsum; 1ZW7; -.
DR   PDBsum; 2G3Q; -.
DR   PDBsum; 2JT4; -.
DR   PDBsum; 2JWZ; -.
DR   PDBsum; 2KDI; -.
DR   PDBsum; 2L00; -.
DR   PDBsum; 3CMM; -.
DR   PDBsum; 3L0W; -.
DR   PDBsum; 3L10; -.
DR   PDBsum; 3OLM; -.
DR   PDBsum; 4HCN; -.
DR   PDBsum; 4NNJ; -.
DR   PDBsum; 4Q5E; -.
DR   PDBsum; 4Q5H; -.
DR   BMRB; P0CG63; -.
DR   SMR; P0CG63; -.
DR   BioGRID; 31215; 542.
DR   IntAct; P0CG63; 151.
DR   MINT; P0CG63; -.
DR   STRING; 4932.YLL039C; -.
DR   iPTMnet; P0CG63; -.
DR   SWISS-2DPAGE; P61864; -.
DR   MaxQB; P0CG63; -.
DR   PaxDb; P0CG63; -.
DR   PRIDE; P0CG63; -.
DR   TopDownProteomics; P0CG63; -.
DR   EnsemblFungi; YLL039C_mRNA; YLL039C; YLL039C.
DR   GeneID; 850620; -.
DR   KEGG; sce:YLL039C; -.
DR   SGD; S000003962; UBI4.
DR   VEuPathDB; FungiDB:YLL039C; -.
DR   eggNOG; KOG0001; Eukaryota.
DR   GeneTree; ENSGT00940000162439; -.
DR   HOGENOM; CLU_010412_7_0_1; -.
DR   InParanoid; P0CG63; -.
DR   OMA; VHENTRR; -.
DR   Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR   Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-SCE-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-SCE-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR   Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR   Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-SCE-5689603; UCH proteinases.
DR   Reactome; R-SCE-5689877; Josephin domain DUBs.
DR   Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR   Reactome; R-SCE-5689901; Metalloprotease DUBs.
DR   Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR   Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR   Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-SCE-72649; Translation initiation complex formation.
DR   Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-SCE-8948747; Regulation of PTEN localization.
DR   Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-SCE-901032; ER Quality Control Compartment (ERQC).
DR   Reactome; R-SCE-9020702; Interleukin-1 signaling.
DR   Reactome; R-SCE-9033241; Peroxisomal protein import.
DR   Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-SCE-9646399; Aggrephagy.
DR   Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   EvolutionaryTrace; P0CG63; -.
DR   PRO; PR:P0CG63; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P0CG63; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031386; F:protein tag; IDA:FlyBase.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 5.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 5.
DR   SUPFAM; SSF54236; SSF54236; 5.
DR   PROSITE; PS00299; UBIQUITIN_1; 5.
DR   PROSITE; PS50053; UBIQUITIN_2; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW   Repeat; Ubl conjugation.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396306"
FT   CHAIN           77..152
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396307"
FT   CHAIN           153..228
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396308"
FT   CHAIN           229..304
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396309"
FT   CHAIN           305..380
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396310"
FT   PROPEP          381
FT                   /id="PRO_0000396311"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          77..152
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          153..228
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          229..304
FT                   /note="Ubiquitin-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          305..380
FT                   /note="Ubiquitin-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:7862120"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   MUTAGEN         29
FT                   /note="K->R: Deficiency in ubiquitin-protein conjugate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:7615550"
FT   MUTAGEN         48
FT                   /note="K->R: Deficiency in ubiquitin-protein conjugate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:7615550,
FT                   ECO:0000269|PubMed:7862120"
FT   MUTAGEN         63
FT                   /note="K->R: Deficiency in ubiquitin-protein conjugate
FT                   formation. Loss of DNA repair function."
FT                   /evidence="ECO:0000269|PubMed:7615550"
FT   CONFLICT        352
FT                   /note="K -> N (in Ref. 4; CAA25706)"
FT                   /evidence="ECO:0000305"
FT   STRAND          231..234
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   STRAND          241..243
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   HELIX           251..256
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   STRAND          274..277
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   HELIX           285..287
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:1ZW7"
FT   STRAND          306..310
FT                   /evidence="ECO:0007829|PDB:4Q5E"
FT   TURN            312..314
FT                   /evidence="ECO:0007829|PDB:1Q0W"
FT   STRAND          316..320
FT                   /evidence="ECO:0007829|PDB:4Q5E"
FT   STRAND          323..326
FT                   /evidence="ECO:0007829|PDB:1Q0W"
FT   HELIX           327..338
FT                   /evidence="ECO:0007829|PDB:4Q5E"
FT   TURN            342..344
FT                   /evidence="ECO:0007829|PDB:4Q5E"
FT   STRAND          345..349
FT                   /evidence="ECO:0007829|PDB:4Q5E"
FT   STRAND          351..353
FT                   /evidence="ECO:0007829|PDB:4NNJ"
FT   STRAND          358..360
FT                   /evidence="ECO:0007829|PDB:3OLM"
FT   HELIX           361..363
FT                   /evidence="ECO:0007829|PDB:4Q5E"
FT   STRAND          370..375
FT                   /evidence="ECO:0007829|PDB:4Q5E"
FT   HELIX           377..379
FT                   /evidence="ECO:0007829|PDB:2JT4"
SQ   SEQUENCE   381 AA;  42826 MW;  68C6235F9909A2AE CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKSKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKS
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVESSDT IDNVKSKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
     LRGGMQIFVK TLTGKTITLE VESSDTIDNV KSKIQDKEGI PPDQQRLIFA GKQLEDGRTL
     SDYNIQKEST LHLVLRLRGG N
//
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