GenomeNet

Database: UniProt
Entry: EIF2D_HUMAN
LinkDB: EIF2D_HUMAN
Original site: EIF2D_HUMAN 
ID   EIF2D_HUMAN             Reviewed;         584 AA.
AC   P41214; Q5SY40; Q8IXV3; Q96DG3; Q96TG7; Q9NR27; Q9NSN0; Q9NV18;
AC   Q9NZ21;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 3.
DT   27-SEP-2017, entry version 158.
DE   RecName: Full=Eukaryotic translation initiation factor 2D;
DE            Short=eIF2d;
DE   AltName: Full=Hepatocellular carcinoma-associated antigen 56;
DE   AltName: Full=Ligatin;
GN   Name=EIF2D; Synonyms=HCA56, LGTN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP   SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20566627; DOI=10.1074/jbc.M110.119693;
RA   Dmitriev S.E., Terenin I.M., Andreev D.E., Ivanov P.A.,
RA   Dunaevsky J.E., Merrick W.C., Shatsky I.N.;
RT   "GTP-independent tRNA delivery to the ribosomal P-site by a novel
RT   eukaryotic translation factor.";
RL   J. Biol. Chem. 285:26779-26787(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Hepatoma;
RX   PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA   Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA   Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA   Chen W.-F.;
RT   "Large scale identification of human hepatocellular carcinoma-
RT   associated antigens by autoantibodies.";
RL   J. Immunol. 169:1102-1109(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix, Lymph, and Testis;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-584 (ISOFORM 1).
RC   TISSUE=Testis;
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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 234-308.
RX   PubMed=2482295;
RA   Jakoi E.R., Brown A.L., Ho Y.S., Snyderman R.;
RT   "Molecular cloning of the cDNA for ligatin.";
RL   J. Cell Sci. 93:227-232(1989).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
RP   FUNCTION.
RX   PubMed=20713520; DOI=10.1101/gad.1957510;
RA   Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U.,
RA   Pestova T.V.;
RT   "Activities of ligatin and MCT-1/DENR in eukaryotic translation
RT   initiation and ribosomal recycling.";
RL   Genes Dev. 24:1787-1801(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
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.,
RA   Buerckstuemmer T., 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   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-361, 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).
CC   -!- FUNCTION: Translation initiation factor that is able to deliver
CC       tRNA to the P-site of the eukaryotic ribosome in a GTP-independent
CC       manner. The binding of Met-tRNA(I) occurs after the AUG codon
CC       finds its position in the P-site of 40S ribosomes, the situation
CC       that takes place during initiation complex formation on some
CC       specific RNAs. Its activity in tRNA binding with 40S subunits does
CC       not require the presence of the aminoacyl moiety. Possesses the
CC       unique ability to deliver non-Met (elongator) tRNAs into the P-
CC       site of the 40S subunit. In addition to its role in initiation,
CC       can promote release of deacylated tRNA and mRNA from recycled 40S
CC       subunits following ABCE1-mediated dissociation of post-termination
CC       ribosomal complexes into subunits. {ECO:0000269|PubMed:20566627,
CC       ECO:0000269|PubMed:20713520}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20566627}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P41214-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P41214-2; Sequence=VSP_006300;
CC   -!- DEVELOPMENTAL STAGE: Found during embryonic development and in
CC       early differentiated states.
CC   -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
CC   -!- CAUTION: Was previously erroneously called ligatin, a trafficking
CC       receptor for phosphoglycoproteins, while ligatin is actually a
CC       distinct 10 kDa filamentous membrane protein encoded by a still
CC       unidentified gene. {ECO:0000305|PubMed:20566627}.
DR   EMBL; AF220417; AAF34185.2; -; mRNA.
DR   EMBL; AF262403; AAF74205.1; -; mRNA.
DR   EMBL; AK001852; BAA91942.1; -; mRNA.
DR   EMBL; AL591846; CAI13533.1; -; Genomic_DNA.
DR   EMBL; AL591846; CAI13534.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93536.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93540.1; -; Genomic_DNA.
DR   EMBL; BC001585; AAH01585.1; -; mRNA.
DR   EMBL; BC039134; AAH39134.2; -; mRNA.
DR   EMBL; BC058905; AAH58905.1; -; mRNA.
DR   EMBL; AL162001; CAB82330.1; -; mRNA.
DR   EMBL; AF159586; AAD41909.1; -; mRNA.
DR   CCDS; CCDS1465.1; -. [P41214-1]
DR   CCDS; CCDS55680.1; -. [P41214-2]
DR   PIR; A60697; A60697.
DR   PIR; T47178; T47178.
DR   RefSeq; NP_001188407.1; NM_001201478.1. [P41214-2]
DR   RefSeq; NP_008824.2; NM_006893.2. [P41214-1]
DR   UniGene; Hs.497581; -.
DR   ProteinModelPortal; P41214; -.
DR   SMR; P41214; -.
DR   BioGrid; 108259; 24.
DR   IntAct; P41214; 2.
DR   MINT; MINT-3015310; -.
DR   STRING; 9606.ENSP00000271764; -.
DR   iPTMnet; P41214; -.
DR   PhosphoSitePlus; P41214; -.
DR   BioMuta; EIF2D; -.
DR   DMDM; 158957575; -.
DR   EPD; P41214; -.
DR   MaxQB; P41214; -.
DR   PaxDb; P41214; -.
DR   PeptideAtlas; P41214; -.
DR   PRIDE; P41214; -.
DR   DNASU; 1939; -.
DR   Ensembl; ENST00000271764; ENSP00000271764; ENSG00000143486. [P41214-1]
DR   Ensembl; ENST00000367114; ENSP00000356081; ENSG00000143486. [P41214-2]
DR   GeneID; 1939; -.
DR   KEGG; hsa:1939; -.
DR   UCSC; uc001heh.4; human. [P41214-1]
DR   CTD; 1939; -.
DR   EuPathDB; HostDB:ENSG00000143486.15; -.
DR   GeneCards; EIF2D; -.
DR   HGNC; HGNC:6583; EIF2D.
DR   HPA; HPA028220; -.
DR   MIM; 613709; gene.
DR   neXtProt; NX_P41214; -.
DR   OpenTargets; ENSG00000143486; -.
DR   PharmGKB; PA30355; -.
DR   eggNOG; KOG2522; Eukaryota.
DR   eggNOG; ENOG410XSAV; LUCA.
DR   GeneTree; ENSGT00550000074865; -.
DR   HOVERGEN; HBG006268; -.
DR   InParanoid; P41214; -.
DR   KO; K15027; -.
DR   OMA; REQPYHP; -.
DR   OrthoDB; EOG091G0DTH; -.
DR   PhylomeDB; P41214; -.
DR   TreeFam; TF105830; -.
DR   ChiTaRS; EIF2D; human.
DR   GeneWiki; LGTN; -.
DR   GenomeRNAi; 1939; -.
DR   PRO; PR:P41214; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000143486; -.
DR   ExpressionAtlas; P41214; baseline and differential.
DR   Genevisible; P41214; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IDA:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR   GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR   GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB.
DR   Gene3D; 1.10.245.10; -; 1.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.30.780.10; -; 1.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_domain.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   Pfam; PF01253; SUI1; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF47592; SSF47592; 1.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW   Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    584       Eukaryotic translation initiation factor
FT                                2D.
FT                                /FTId=PRO_0000130611.
FT   DOMAIN       93    173       PUA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00161}.
FT   DOMAIN      491    564       SUI1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00200}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES     237    237       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     254    254       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61211}.
FT   MOD_RES     361    361       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ     177    300       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12097419}.
FT                                /FTId=VSP_006300.
FT   VARIANT     210    210       T -> I (in dbSNP:rs35252702).
FT                                /FTId=VAR_052507.
FT   CONFLICT     11     11       N -> D (in Ref. 3; BAA91942).
FT                                {ECO:0000305}.
FT   CONFLICT     66     66       S -> N (in Ref. 2; AAF34185/AAF74205).
FT                                {ECO:0000305}.
FT   CONFLICT    210    210       T -> N (in Ref. 2; AAF34185).
FT                                {ECO:0000305}.
FT   CONFLICT    304    308       GRQLD -> DDNWT (in Ref. 8; AAD41909).
FT                                {ECO:0000305}.
SQ   SEQUENCE   584 AA;  64706 MW;  C302B63268231154 CRC64;
     MFAKAFRVKS NTAIKGSDRR KLRADVTTAF PTLGTDQVSE LVPGKEELNI VKLYAHKGDA
     VTVYVSGGNP ILFELEKNLY PTVYTLWSYP DLLPTFTTWP LVLEKLVGGA DLMLPGLVMP
     PAGLPQVQKG DLCAISLVGN RAPVAIGVAA MSTAEMLTSG LKGRGFSVLH TYQDHLWRSG
     NKSSPPSIAP LALDSADLSE EKGSVQMDST LQGDMRHMTL EGEEENGEVH QAREDKSLSE
     APEDTSTRGL NQDSTDSKTL QEQMDELLQQ CFLHALKCRV KKADLPLLTS TFLGSHMFSC
     CPEGRQLDIK KSSYKKLSKF LQQMQQEQII QVKELSKGVE SIVAVDWKHP RITSFVIPEP
     SPTSQTIQEG SREQPYHPPD IKPLYCVPAS MTLLFQESGH KKGSFLEGSE VRTIVINYAK
     KNDLVDADNK NLVRLDPILC DCILEKNEQH TVMKLPWDSL LTRCLEKLQP AYQVTLPGQE
     PIVKKGRICP IDITLAQRAS NKKVTVVRNL EAYGLDPYSV AAILQQRCQA STTVNPAPGA
     KDSLQVQIQG NQVHHLGWLL LEEYQLPRKH IQGLEKALKP GKKK
//
DBGET integrated database retrieval system