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Database: UniProt
Entry: P32019
LinkDB: P32019
Original site: P32019 
ID   I5P2_HUMAN              Reviewed;         993 AA.
AC   P32019; C9J6U5; Q5VSG9; Q5VSH0; Q5VSH1; Q658Q5; Q6P6D4; Q6PD53;
AC   Q86YE1;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 4.
DT   03-SEP-2014, entry version 136.
DE   RecName: Full=Type II inositol 1,4,5-trisphosphate 5-phosphatase;
DE            EC=3.1.3.36;
DE   AltName: Full=75 kDa inositol polyphosphate-5-phosphatase;
DE   AltName: Full=Phosphoinositide 5-phosphatase;
DE            Short=5PTase;
DE   Flags: Precursor;
GN   Name=INPP5B; Synonyms=OCRL2;
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 2), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-990, MUTAGENESIS OF
RP   CYS-990, AND VARIANT THR-745.
RX   PubMed=7721860; DOI=10.1074/jbc.270.16.9370;
RA   Jefferson A.B., Majerus P.W.;
RT   "Properties of type II inositol polyphosphate 5-phosphatase.";
RL   J. Biol. Chem. 270:9370-9377(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT
RP   THR-745.
RC   TISSUE=Lymph;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-178.
RC   TISSUE=Stomach;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 284-954, PROTEIN SEQUENCE OF 321-339,
RP   AND VARIANT THR-745.
RC   TISSUE=Placenta;
RX   PubMed=1718960;
RA   Ross T.S., Jefferson A.B., Mitchell C.A., Majerus P.W.;
RT   "Cloning and expression of human 75-kDa inositol polyphosphate-5-
RT   phosphatase.";
RL   J. Biol. Chem. 266:20283-20289(1991).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH RAB GTPASES.
RX   PubMed=17956944; DOI=10.1242/jcs.014423;
RA   Williams C., Choudhury R., McKenzie E., Lowe M.;
RT   "Targeting of the type II inositol polyphosphate 5-phosphatase INPP5B
RT   to the early secretory pathway.";
RL   J. Cell Sci. 120:3941-3951(2007).
RN   [7]
RP   INTERACTION WITH FAM109A.
RX   PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA   Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT   "Two closely related endocytic proteins that share a common OCRL-
RT   binding motif with APPL1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
RN   [8]
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   [9]
RP   INTERACTION WITH FAM109A AND FAM109B.
RX   PubMed=21233288; DOI=10.1091/mbc.E10-08-0730;
RA   Noakes C.J., Lee G., Lowe M.;
RT   "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling
RT   in the endocytic pathway.";
RL   Mol. Biol. Cell 22:606-623(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 339-646 IN COMPLEX WITH
RP   MAGNESIUM AND PHOSPHATIDYLINOSITOL 4-PHOSPHATE.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of INPP5B in complex with phosphatidylinositol 4-
RT   phosphate (CASP target).";
RL   Submitted (JUL-2010) to the PDB data bank.
CC   -!- FUNCTION: Hydrolyzes phosphatidylinositol 4,5-bisphosphate
CC       (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol
CC       1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates
CC       cellular signaling events.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate
CC       + phosphate.
CC   -!- SUBUNIT: Interacts with APPL1, FAM109A and FAM109B. Interacts with
CC       several Rab GTPases, at least RAB1A, RAB2A, RAB5A, RAB6A, RAB8A,
CC       RAB9A and RAB33B; these interactions may play a dual role in
CC       targeting INPP5B to the specific membranes and stimulating the
CC       phosphatase activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum-
CC       Golgi intermediate compartment. Early endosome membrane. Membrane;
CC       Peripheral membrane protein; Cytoplasmic side. Cytoplasmic
CC       vesicle, phagosome membrane (By similarity). Golgi apparatus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P32019-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=P32019-2; Sequence=VSP_012820;
CC       Name=3;
CC         IsoId=P32019-3; Sequence=VSP_012821;
CC       Name=4;
CC         IsoId=P32019-4; Sequence=VSP_013902, VSP_013903;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Platelets.
CC   -!- DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase
CC       activating) domains form a single folding module. The ASH domain
CC       has an immunoglobulin-like fold, the Rho-GAP domain lacks the
CC       catalytic arginine and is catalytically inactive. The ASH-RhoGAP
CC       module regulates the majority of the protein-protein interactions
CC       currently described. The ASH domain mediates association with
CC       membrane-targeting Rab GTPases. The Rho-GAP domain interacts with
CC       the endocytic adapter APPL1, which is then displaced by FAM109A
CC       and FAM109B as endosomes mature, all three interactions relie on
CC       F&H motifs, an approximately 12-13 amino-acid sequence centered
CC       around Phe and His residues essential for binding (By similarity).
CC   -!- PTM: Isoprenylation at Cys-990 may be required for localization at
CC       the membrane.
CC   -!- PTM: May be proteolytically cleaved after Lys-320 as inferred from
CC       N-terminal protein sequence of the 75 kda form (PubMed:1718960).
CC   -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
CC       phosphatase type II family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA79207.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; M74161; AAA79207.1; ALT_INIT; mRNA.
DR   EMBL; AL603790; CAH69926.1; -; Genomic_DNA.
DR   EMBL; AL929472; CAH69926.1; JOINED; Genomic_DNA.
DR   EMBL; AL603790; CAH69928.1; -; Genomic_DNA.
DR   EMBL; AL929472; CAH69928.1; JOINED; Genomic_DNA.
DR   EMBL; AL603790; CAH69929.1; -; Genomic_DNA.
DR   EMBL; AL929472; CAH69929.1; JOINED; Genomic_DNA.
DR   EMBL; AL929472; CAH70076.1; -; Genomic_DNA.
DR   EMBL; AL603790; CAH70076.1; JOINED; Genomic_DNA.
DR   EMBL; AL929472; CAH70079.1; -; Genomic_DNA.
DR   EMBL; AL603790; CAH70079.1; JOINED; Genomic_DNA.
DR   EMBL; AL929472; CAH70080.1; -; Genomic_DNA.
DR   EMBL; AL603790; CAH70080.1; JOINED; Genomic_DNA.
DR   EMBL; BX296560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC042529; AAH42529.2; -; mRNA.
DR   EMBL; BC058932; AAH58932.1; -; mRNA.
DR   EMBL; AL833055; CAH56301.1; -; mRNA.
DR   CCDS; CCDS41306.1; -. [P32019-2]
DR   RefSeq; NP_005531.2; NM_005540.2. [P32019-2]
DR   RefSeq; XP_005270893.1; XM_005270836.1. [P32019-3]
DR   UniGene; Hs.449942; -.
DR   PDB; 3MTC; X-ray; 2.40 A; A=339-643.
DR   PDB; 3N9V; X-ray; 2.65 A; A/B=342-646.
DR   PDB; 4CML; X-ray; 2.30 A; A=339-643.
DR   PDBsum; 3MTC; -.
DR   PDBsum; 3N9V; -.
DR   PDBsum; 4CML; -.
DR   ProteinModelPortal; P32019; -.
DR   SMR; P32019; 1-155, 339-643, 656-989.
DR   BioGrid; 109845; 2.
DR   STRING; 9606.ENSP00000362115; -.
DR   PhosphoSite; P32019; -.
DR   DMDM; 281185510; -.
DR   MaxQB; P32019; -.
DR   PaxDb; P32019; -.
DR   PRIDE; P32019; -.
DR   Ensembl; ENST00000373023; ENSP00000362114; ENSG00000204084. [P32019-1]
DR   Ensembl; ENST00000373024; ENSP00000362115; ENSG00000204084. [P32019-2]
DR   Ensembl; ENST00000373026; ENSP00000362117; ENSG00000204084. [P32019-1]
DR   Ensembl; ENST00000373027; ENSP00000362118; ENSG00000204084. [P32019-3]
DR   GeneID; 3633; -.
DR   KEGG; hsa:3633; -.
DR   UCSC; uc001ccf.1; human. [P32019-1]
DR   UCSC; uc001ccg.1; human. [P32019-2]
DR   CTD; 3633; -.
DR   GeneCards; GC01M038326; -.
DR   HGNC; HGNC:6077; INPP5B.
DR   HPA; HPA028803; -.
DR   MIM; 147264; gene.
DR   neXtProt; NX_P32019; -.
DR   PharmGKB; PA29885; -.
DR   eggNOG; COG5411; -.
DR   HOVERGEN; HBG000070; -.
DR   InParanoid; P32019; -.
DR   KO; K01099; -.
DR   OMA; PMEIPKE; -.
DR   OrthoDB; EOG7J4465; -.
DR   PhylomeDB; P32019; -.
DR   TreeFam; TF317034; -.
DR   BioCyc; MetaCyc:HS05898-MONOMER; -.
DR   BRENDA; 3.1.3.36; 2681.
DR   Reactome; REACT_11051; Rho GTPase cycle.
DR   Reactome; REACT_150312; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; REACT_150352; Synthesis of IP2, IP, and Ins in the cytosol.
DR   SABIO-RK; P32019; -.
DR   ChiTaRS; INPP5B; human.
DR   EvolutionaryTrace; P32019; -.
DR   GeneWiki; INPP5B; -.
DR   GenomeRNAi; 3633; -.
DR   NextBio; 14219; -.
DR   PRO; PR:P32019; -.
DR   ArrayExpress; P32019; -.
DR   Bgee; P32019; -.
DR   CleanEx; HS_INPP5B; -.
DR   Genevestigator; P32019; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0070613; P:regulation of protein processing; IEA:Ensembl.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0030317; P:sperm motility; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 2.
DR   SUPFAM; SSF56219; SSF56219; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW   Cytoplasmic vesicle; Direct protein sequencing; Endosome;
KW   Golgi apparatus; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Methylation; Polymorphism; Prenylation;
KW   Reference proteome.
FT   CHAIN         1    990       Type II inositol 1,4,5-trisphosphate 5-
FT                                phosphatase.
FT                                /FTId=PRO_0000015640.
FT   PROPEP      991    993       Removed in mature form (Potential).
FT                                /FTId=PRO_0000422293.
FT   DOMAIN       22    148       PH.
FT   DOMAIN      821    993       Rho-GAP.
FT   REGION      342    668       5-phosphatase (By similarity).
FT   REGION      459    460       Substrate binding.
FT   REGION      582    583       Substrate binding.
FT   REGION      596    598       Substrate binding.
FT   REGION      669    782       ASH (By similarity).
FT   METAL       355    355       Magnesium.
FT   METAL       383    383       Magnesium.
FT   BINDING     383    383       Substrate.
FT   MOD_RES     990    990       Cysteine methyl ester (Potential).
FT   LIPID       990    990       S-farnesyl cysteine (Potential).
FT   VAR_SEQ       1    244       Missing (in isoform 3).
FT                                /FTId=VSP_012821.
FT   VAR_SEQ     178    257       Missing (in isoform 2).
FT                                /FTId=VSP_012820.
FT   VAR_SEQ     810    828       TLMPVWTGDDGSQLDSPME -> LAYLAAYCFETQLVTKSL
FT                                I (in isoform 4).
FT                                /FTId=VSP_013902.
FT   VAR_SEQ     829    993       Missing (in isoform 4).
FT                                /FTId=VSP_013903.
FT   VARIANT      46     46       G -> S (in dbSNP:rs56993041).
FT                                /FTId=VAR_061270.
FT   VARIANT     745    745       M -> T (in dbSNP:rs11488569).
FT                                /FTId=VAR_028002.
FT   MUTAGEN     990    990       C->S: Loss of prenylation and membrane
FT                                localization.
FT   CONFLICT    587    606       GSDDWDTSEKCRAPAWCDRI -> RALTTGIPVRSAVLLPG
FT                                VIGF (in Ref. 5; AA sequence).
FT   CONFLICT    911    911       G -> P (in Ref. 5; AA sequence).
FT   STRAND      340    353
FT   HELIX       364    367
FT   STRAND      368    370
FT   STRAND      375    382
FT   HELIX       388    391
FT   HELIX       397    409
FT   STRAND      416    424
FT   STRAND      427    434
FT   HELIX       435    440
FT   STRAND      441    450
FT   HELIX       453    455
FT   STRAND      460    469
FT   STRAND      472    480
FT   HELIX       485    487
FT   HELIX       488    501
FT   STRAND      509    511
FT   STRAND      518    527
FT   HELIX       537    545
FT   HELIX       549    553
FT   HELIX       557    563
FT   STRAND      588    591
FT   STRAND      604    620
FT   STRAND      626    629
FT   STRAND      632    643
SQ   SEQUENCE   993 AA;  112852 MW;  ABD3581CC6CD29D6 CRC64;
     MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH ALFLYTHRRM
     AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ LDTAELSLVF QLPFGSQTRM
     FLHEVARACP GFDSATRDPE FLWLSRYRCA ELELEMPTPR GCNSALVTWP GYATIGGGRY
     PSRKKRWGLE EARPQGAGSV LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE
     AGREMSAAAG SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD
     MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG TYNVNGQSPK
     ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSEGL HPDAKYAKVK
     LIRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQFH NTSICVVNSH
     LAAHIEEYER RNQDYKDICS RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV
     KKLIEEKDFQ MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP
     AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK TLEEIVRSLD
     KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP CHFEFINKPD EESYCKQWLN
     ANPSRGFLLP DSDVEIDLEL FVNKMTATKL NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL
     PSCFGSPIHT LCYMREPILD LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL
     YRNAVQQEDL FQQPGLRSEF EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY
     STYHNCLECS GNYTASKQVI STLPIFHKNV FHYLMAFLRE LLKNSAKNHL DENILASIFG
     SLLLRNPAGH QKLDMTEKKK AQEFIHQFLC NPL
//
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