GenomeNet

Database: UniProt
Entry: Q9H8H2
LinkDB: Q9H8H2
Original site: Q9H8H2 
ID   DDX31_HUMAN             Reviewed;         851 AA.
AC   Q9H8H2; Q5K6N2; Q5K6N3; Q5K6N4; Q5VZJ4; Q5VZJ9; Q96E91; Q96NY2;
AC   Q96SX5; Q9H5K6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   16-OCT-2019, entry version 158.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX31;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 31;
DE   AltName: Full=Helicain;
GN   Name=DDX31;
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).
RX   PubMed=12782131; DOI=10.1016/s0888-7543(03)00049-1;
RA   Abdelhaleem M., Maltais L., Wain H.;
RT   "The human DDX and DHX gene families of putative RNA helicases.";
RL   Genomics 81:618-622(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT VAL-799.
RA   Sugihara T.T., Wadhwa R.R.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 90-851 (ISOFORM 1), AND VARIANT
RP   VAL-799.
RC   TISSUE=Hepatoma, Placenta, and Teratocarcinoma;
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=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-851 (ISOFORM 1), AND
RP   VARIANT VAL-799.
RC   TISSUE=Lung;
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   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA   Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA   Greco A., Hochstrasser D.F., Diaz J.-J.;
RT   "Functional proteomic analysis of human nucleolus.";
RL   Mol. Biol. Cell 13:4100-4109(2002).
RN   [7]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH NPM1, AND
RP   FUNCTION.
RX   PubMed=23019224; DOI=10.1158/0008-5472.can-12-1645;
RA   Fukawa T., Ono M., Matsuo T., Uehara H., Miki T., Nakamura Y.,
RA   Kanayama H.O., Katagiri T.;
RT   "DDX31 regulates the p53-HDM2 pathway and rRNA gene transcription
RT   through its interaction with NPM1 in renal cell carcinomas.";
RL   Cancer Res. 72:5867-5877(2012).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-828, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Probable ATP-dependent RNA helicase (By similarity).
CC       Plays a role in ribosome biogenesis and TP53/p53 regulation
CC       through its interaction with NPM1 (PubMed:23019224). {ECO:0000250,
CC       ECO:0000269|PubMed:23019224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Interacts with NPM1; this interaction prevents
CC       interaction between NPM1 and HDM2. {ECO:0000269|PubMed:23019224}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:23019224}.
CC       Note=Colocalized with NPM1 in the nucleoli.
CC       {ECO:0000269|PubMed:23019224}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Helicain B;
CC         IsoId=Q9H8H2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Helicain C;
CC         IsoId=Q9H8H2-2; Sequence=VSP_014790;
CC         Note=No experimental confirmation available.;
CC       Name=3; Synonyms=Helicain A;
CC         IsoId=Q9H8H2-3; Sequence=VSP_014787, VSP_014788;
CC       Name=4;
CC         IsoId=Q9H8H2-4; Sequence=VSP_014789;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Weakly or undetectably expressed in normal
CC       organs. Up-regulated in renal cell carcinoma.
CC       {ECO:0000269|PubMed:23019224}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ14889.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAQ14890.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB14644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB15620.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AF427339; AAL26549.1; -; mRNA.
DR   EMBL; AF335567; AAQ14888.1; -; mRNA.
DR   EMBL; AF335568; AAQ14889.1; ALT_FRAME; mRNA.
DR   EMBL; AF335569; AAQ14890.1; ALT_FRAME; mRNA.
DR   EMBL; AK023695; BAB14644.1; ALT_INIT; mRNA.
DR   EMBL; AK027002; BAB15620.1; ALT_FRAME; mRNA.
DR   EMBL; AK027484; BAB55146.1; -; mRNA.
DR   EMBL; AL160165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012726; AAH12726.2; -; mRNA.
DR   CCDS; CCDS6951.1; -. [Q9H8H2-1]
DR   CCDS; CCDS6952.1; -. [Q9H8H2-4]
DR   CCDS; CCDS83433.1; -. [Q9H8H2-3]
DR   RefSeq; NP_001309269.1; NM_001322340.1. [Q9H8H2-2]
DR   RefSeq; NP_001309273.1; NM_001322344.1. [Q9H8H2-3]
DR   RefSeq; NP_073616.6; NM_022779.8. [Q9H8H2-1]
DR   RefSeq; NP_619526.1; NM_138620.1. [Q9H8H2-4]
DR   SMR; Q9H8H2; -.
DR   BioGrid; 122302; 118.
DR   IntAct; Q9H8H2; 103.
DR   MINT; Q9H8H2; -.
DR   STRING; 9606.ENSP00000361232; -.
DR   iPTMnet; Q9H8H2; -.
DR   PhosphoSitePlus; Q9H8H2; -.
DR   BioMuta; DDX31; -.
DR   DMDM; 71153334; -.
DR   SWISS-2DPAGE; Q9H8H2; -.
DR   EPD; Q9H8H2; -.
DR   jPOST; Q9H8H2; -.
DR   MassIVE; Q9H8H2; -.
DR   MaxQB; Q9H8H2; -.
DR   PaxDb; Q9H8H2; -.
DR   PeptideAtlas; Q9H8H2; -.
DR   PRIDE; Q9H8H2; -.
DR   ProteomicsDB; 81209; -. [Q9H8H2-1]
DR   ProteomicsDB; 81210; -. [Q9H8H2-2]
DR   ProteomicsDB; 81211; -. [Q9H8H2-3]
DR   ProteomicsDB; 81212; -. [Q9H8H2-4]
DR   DNASU; 64794; -.
DR   Ensembl; ENST00000310532; ENSP00000310539; ENSG00000125485. [Q9H8H2-4]
DR   Ensembl; ENST00000372153; ENSP00000361226; ENSG00000125485. [Q9H8H2-1]
DR   Ensembl; ENST00000372159; ENSP00000361232; ENSG00000125485. [Q9H8H2-1]
DR   Ensembl; ENST00000480876; ENSP00000479697; ENSG00000125485. [Q9H8H2-3]
DR   GeneID; 64794; -.
DR   KEGG; hsa:64794; -.
DR   UCSC; uc004cbq.1; human. [Q9H8H2-1]
DR   CTD; 64794; -.
DR   DisGeNET; 64794; -.
DR   GeneCards; DDX31; -.
DR   HGNC; HGNC:16715; DDX31.
DR   HPA; HPA020891; -.
DR   MIM; 616533; gene.
DR   neXtProt; NX_Q9H8H2; -.
DR   OpenTargets; ENSG00000125485; -.
DR   PharmGKB; PA27218; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   eggNOG; ENOG410XNT7; LUCA.
DR   GeneTree; ENSGT00550000075041; -.
DR   InParanoid; Q9H8H2; -.
DR   KO; K14806; -.
DR   OMA; FSRIQWL; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q9H8H2; -.
DR   TreeFam; TF323273; -.
DR   ChiTaRS; DDX31; human.
DR   GeneWiki; DDX31; -.
DR   GenomeRNAi; 64794; -.
DR   Pharos; Q9H8H2; -.
DR   PRO; PR:Q9H8H2; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000125485; Expressed in 162 organ(s), highest expression level in left lobe of thyroid gland.
DR   ExpressionAtlas; Q9H8H2; baseline and differential.
DR   Genevisible; Q9H8H2; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Complete proteome; Helicase;
KW   Hydrolase; Methylation; Nucleotide-binding; Nucleus; Polymorphism;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1    851       Probable ATP-dependent RNA helicase
FT                                DDX31.
FT                                /FTId=PRO_0000055049.
FT   DOMAIN      262    443       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      480    659       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     275    282       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       230    259       Q motif.
FT   MOTIF       388    391       DEAD box.
FT   MOD_RES     828    828       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   VAR_SEQ     302    319       RSDGPYALVLVPTRELAL -> VLLLSTFYEEEQRLRKVK
FT                                (in isoform 3). {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_014787.
FT   VAR_SEQ     320    851       Missing (in isoform 3).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_014788.
FT   VAR_SEQ     586    851       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_014789.
FT   VAR_SEQ     603    714       YNAPSSPAEYIHRIGRTARIGCHGSSLLILAPSEAEYVNSL
FT                                ASHKINVSEIKMEDILCVLTRDDCFKGKRWGAQKSHAVGPQ
FT                                EIRERATVLQTVFEDYVHSSERRVSWAKKA -> NTSTGLE
FT                                EPPGLAAMGAACSFWLLRRQNMSTRWLLTKST (in
FT                                isoform 2). {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_014790.
FT   VARIANT     153    153       E -> K (in dbSNP:rs17402080).
FT                                /FTId=VAR_052164.
FT   VARIANT     687    687       R -> Q (in dbSNP:rs34246652).
FT                                /FTId=VAR_052165.
FT   VARIANT     799    799       I -> V (in dbSNP:rs306547).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_023065.
FT   VARIANT     843    843       R -> Q (in dbSNP:rs306548).
FT                                /FTId=VAR_023066.
FT   CONFLICT    206    206       K -> L (in Ref. 3; BAB15620).
FT                                {ECO:0000305}.
FT   CONFLICT    406    406       L -> P (in Ref. 3; BAB15620).
FT                                {ECO:0000305}.
FT   CONFLICT    527    527       Y -> C (in Ref. 3; BAB15620).
FT                                {ECO:0000305}.
FT   CONFLICT    562    562       M -> K (in Ref. 3; BAB55146).
FT                                {ECO:0000305}.
SQ   SEQUENCE   851 AA;  94087 MW;  E3C73701FF2F37E7 CRC64;
     MAPDLASQRH SESFPSVNSR PNVILPGREG RREGLPPGGG TRGSLVPTRP VPPSPAPLGT
     SPYSWSRSGP GRGGGAGSSR VPRGVPGPAV CAPGSLLHHA SPTQTMAAAD GSLFDNPRTF
     SRRPPAQASR QAKATKRKYQ ASSEAPPAKR RNETSFLPAK KTSVKETQRT FKGNAQKMFS
     PKKHSVSTSD RNQEERQCIK TSSLFKNNPD IPELHRPVVK QVQEKVFTSA AFHELGLHPH
     LISTINTVLK MSSMTSVQKQ SIPVLLEGRD ALVRSQTGSG KTLAYCIPVV QSLQAMESKI
     QRSDGPYALV LVPTRELALQ SFDTVQKLLK PFTWIVPGVL MGGEKRKSEK ARLRKGINIL
     ISTPGRLVDH IKSTKNIHFS RLRWLVFDEA DRILDLGFEK DITVILNAVN AECQKRQNVL
     LSATLTEGVT RLADISLHDP VSISVLDKSH DQLNPKDKAV QEVCPPPAGD KLDSFAIPES
     LKQHVTVVPS KLRLVCLAAF ILQKCKFEED QKMVVFFSSC ELVEFHYSLF LQTLLSSSGA
     PASGQLPSAS MRLKFLRLHG GMEQEERTAV FQEFSHSRRG VLLCTDVAAR GLDLPQVTWI
     VQYNAPSSPA EYIHRIGRTA RIGCHGSSLL ILAPSEAEYV NSLASHKINV SEIKMEDILC
     VLTRDDCFKG KRWGAQKSHA VGPQEIRERA TVLQTVFEDY VHSSERRVSW AKKALQSFIQ
     AYATYPRELK HIFHVRSLHL GHVAKSFGLR DAPRNLSALT RKKRKAHVKR PDLHKKTQSK
     HSLAEILRSE YSSGMEADIA KVKKQNAPGE PGGRPLQHSL QPTPCFGRGK TLKWRKTQKG
     VQRDSKTSQK V
//
DBGET integrated database retrieval system