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Database: UniProt
Entry: Q9H3P7
LinkDB: Q9H3P7
Original site: Q9H3P7 
ID   GCP60_HUMAN             Reviewed;         528 AA.
AC   Q9H3P7; B2RB29; Q5VTJ0; Q6P9F1; Q8IZC5; Q8N4D6; Q9H6U3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   01-OCT-2014, entry version 117.
DE   RecName: Full=Golgi resident protein GCP60;
DE   AltName: Full=Acyl-CoA-binding domain-containing protein 3;
DE   AltName: Full=Golgi complex-associated protein 1;
DE            Short=GOCAP1;
DE   AltName: Full=Golgi phosphoprotein 1;
DE            Short=GOLPH1;
DE   AltName: Full=PBR- and PKA-associated protein 7;
DE   AltName: Full=Peripheral benzodiazepine receptor-associated protein PAP7;
GN   Name=ACBD3; Synonyms=GCP60, GOCAP1, GOLPH1;
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], FUNCTION, SUBCELLULAR LOCATION,
RP   INTERACTION WITH GOLGB1, AND TISSUE SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=11590181; DOI=10.1074/jbc.M108961200;
RA   Sohda M., Misumi Y., Yamamoto A., Yano A., Nakamura N., Ikehara Y.;
RT   "Identification and characterization of a novel Golgi protein, GCP60,
RT   that interacts with the integral membrane protein giantin.";
RL   J. Biol. Chem. 276:45298-45306(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-187.
RC   TISSUE=Placenta;
RA   Liu J., Tobin D., Tasken K., Papadopoulos V.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-187.
RC   TISSUE=Trachea;
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Ovary;
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   PROTEIN SEQUENCE OF 2-9.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-20, AND
RP   IDENTIFICATION 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   [11]
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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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).
CC   -!- FUNCTION: Involved in the maintenance of Golgi structure by
CC       interacting with giantin, affecting protein transport between the
CC       endoplasmic reticulum and Golgi. Involved in hormone-induced
CC       steroid biosynthesis in testicular Leydig cells (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the C-terminal cytoplasmic domain of
CC       giantin/GOLGB1. Interacts with PBR and PKA regulatory subunit RI-
CC       alpha. Does not interact with PKA regulatory subunit RI-beta nor
CC       PKA regulatory subunit RII-alpha (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       O91464:- (xeno); NbExp=21; IntAct=EBI-1791792, EBI-7587528;
CC       Q9UBF8:PI4KB; NbExp=4; IntAct=EBI-1791792, EBI-1053214;
CC       Q8BHN0:Ppm1l (xeno); NbExp=3; IntAct=EBI-1791792, EBI-7970002;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Also
CC       mitochondrial (via its interaction with PBR). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in testis
CC       and ovary. {ECO:0000269|PubMed:11590181}.
CC   -!- DOMAIN: The GOLD domain is essential for giantin binding.
CC   -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00573}.
CC   -!- SIMILARITY: Contains 1 GOLD domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00096}.
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DR   EMBL; AB043587; BAB20592.2; -; mRNA.
DR   EMBL; AY150218; AAN60219.1; -; mRNA.
DR   EMBL; AK025520; BAB15159.1; -; mRNA.
DR   EMBL; AK314468; BAG37076.1; -; mRNA.
DR   EMBL; AL592045; CAH71922.1; -; Genomic_DNA.
DR   EMBL; CH471098; EAW69775.1; -; Genomic_DNA.
DR   EMBL; BC034563; AAH34563.2; -; mRNA.
DR   EMBL; BC045533; AAH45533.1; -; mRNA.
DR   EMBL; BC060792; AAH60792.1; -; mRNA.
DR   CCDS; CCDS1551.1; -.
DR   RefSeq; NP_073572.2; NM_022735.3.
DR   UniGene; Hs.520207; -.
DR   ProteinModelPortal; Q9H3P7; -.
DR   SMR; Q9H3P7; 101-162.
DR   BioGrid; 122262; 18.
DR   DIP; DIP-40673N; -.
DR   IntAct; Q9H3P7; 12.
DR   MINT; MINT-5003562; -.
DR   STRING; 9606.ENSP00000355777; -.
DR   BindingDB; Q9H3P7; -.
DR   PhosphoSite; Q9H3P7; -.
DR   DMDM; 51316096; -.
DR   MaxQB; Q9H3P7; -.
DR   PaxDb; Q9H3P7; -.
DR   PeptideAtlas; Q9H3P7; -.
DR   PRIDE; Q9H3P7; -.
DR   Ensembl; ENST00000366812; ENSP00000355777; ENSG00000182827.
DR   GeneID; 64746; -.
DR   KEGG; hsa:64746; -.
DR   UCSC; uc001hpy.3; human.
DR   CTD; 64746; -.
DR   GeneCards; GC01M226332; -.
DR   H-InvDB; HIX0159664; -.
DR   HGNC; HGNC:15453; ACBD3.
DR   HPA; HPA015594; -.
DR   MIM; 606809; gene.
DR   neXtProt; NX_Q9H3P7; -.
DR   PharmGKB; PA28803; -.
DR   eggNOG; NOG287879; -.
DR   HOVERGEN; HBG051712; -.
DR   InParanoid; Q9H3P7; -.
DR   OMA; FGVFFEW; -.
DR   OrthoDB; EOG7KDFB4; -.
DR   PhylomeDB; Q9H3P7; -.
DR   TreeFam; TF321667; -.
DR   ChiTaRS; ACBD3; human.
DR   GeneWiki; ACBD3; -.
DR   GenomeRNAi; 64746; -.
DR   NextBio; 66697; -.
DR   PRO; PR:Q9H3P7; -.
DR   Bgee; Q9H3P7; -.
DR   CleanEx; HS_ACBD3; -.
DR   Genevestigator; Q9H3P7; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   Gene3D; 1.20.80.10; -; 1.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR009038; GOLD.
DR   Pfam; PF00887; ACBP; 1.
DR   Pfam; PF13897; GOLD_2; 1.
DR   SUPFAM; SSF101576; SSF101576; 2.
DR   SUPFAM; SSF47027; SSF47027; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Complete proteome;
KW   Direct protein sequencing; Golgi apparatus; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Mitochondrion; Phosphoprotein;
KW   Polymorphism; Reference proteome; Steroid biosynthesis.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:12665801,
FT                                ECO:0000269|PubMed:22223895,
FT                                ECO:0000269|PubMed:22814378}.
FT   CHAIN         2    528       Golgi resident protein GCP60.
FT                                /FTId=PRO_0000214029.
FT   DOMAIN       83    174       ACB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00573}.
FT   DOMAIN      384    526       GOLD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00096}.
FT   COILED      174    257       {ECO:0000255}.
FT   COMPBIAS     21     60       Pro-rich.
FT   COMPBIAS    182    240       Glu-rich.
FT   COMPBIAS    196    238       Arg-rich.
FT   COMPBIAS    241    308       Gln-rich.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:22223895,
FT                                ECO:0000269|PubMed:22814378}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000269|PubMed:20068231}.
FT   MOD_RES      20     20       Phosphoserine.
FT                                {ECO:0000269|PubMed:20068231}.
FT   MOD_RES      43     43       Phosphoserine.
FT                                {ECO:0000269|PubMed:18691976}.
FT   VARIANT     187    187       E -> D (in dbSNP:rs2306120).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019615.
FT   CONFLICT     93     93       F -> L (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    230    230       R -> I (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    265    265       Q -> R (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    333    333       S -> P (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    384    397       KEKIQQDADSVITV -> QREDSAGCRFRDYS (in Ref.
FT                                2). {ECO:0000305}.
FT   CONFLICT    425    425       Y -> C (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    473    473       K -> R (in Ref. 6; AAH60792).
FT                                {ECO:0000305}.
SQ   SEQUENCE   528 AA;  60593 MW;  B36EC550F8268FC2 CRC64;
     MAAVLNAERL EVSVDGLTLS PDPEERPGAE GAPLLPPPLP PPSPPGSGRG PGASGEQPEP
     GEAAAGGAAE EARRLEQRWG FGLEELYGLA LRFFKEKDGK AFHPTYEEKL KLVALHKQVL
     MGPYNPDTCP EVGFFDVLGN DRRREWAALG NMSKEDAMVE FVKLLNRCCH LFSTYVASHK
     IEKEEQEKKR KEEEERRRRE EEERERLQKE EEKRRREEEE RLRREEEERR RIEEERLRLE
     QQKQQIMAAL NSQTAVQFQQ YAAQQYPGNY EQQQILIRQL QEQHYQQYMQ QLYQVQLAQQ
     QAALQKQQEV VVAGSSLPTS SKVNATVPSN MMSVNGQAKT HTDSSEKELE PEAAEEALEN
     GPKESLPVIA APSMWTRPQI KDFKEKIQQD ADSVITVGRG EVVTVRVPTH EEGSYLFWEF
     ATDNYDIGFG VYFEWTDSPN TAVSVHVSES SDDDEEEEEN IGCEEKAKKN ANKPLLDEIV
     PVYRRDCHEE VYAGSHQYPG RGVYLLKFDN SYSLWRSKSV YYRVYYTR
//
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