GenomeNet

Database: UniProt
Entry: Q9ULI3
LinkDB: Q9ULI3
Original site: Q9ULI3 
ID   HEG1_HUMAN              Reviewed;        1381 AA.
AC   Q9ULI3; Q6NX66; Q8NC40; Q9BSV0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 3.
DT   13-FEB-2019, entry version 133.
DE   RecName: Full=Protein HEG homolog 1;
DE   Flags: Precursor;
GN   Name=HEG1; Synonyms=KIAA1237;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-1381.
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1117-1381.
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 MRNA] OF 682-1381 (ISOFORM 2),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1140-1381 (ISOFORM 1), AND
RP   VARIANT LEU-980.
RC   TISSUE=Kidney, 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   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-159 AND ASN-520.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [6]
RP   GLYCOSYLATION AT THR-67, STRUCTURE OF CARBOHYDRATES, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.M111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of
RT   N-and O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1356-1381 IN COMPLEX WITH
RP   KRIT1, AND INTERACTION WITH KRIT1.
RX   PubMed=23007647; DOI=10.1083/jcb.201205109;
RA   Gingras A.R., Liu J.J., Ginsberg M.H.;
RT   "Structural basis of the junctional anchorage of the cerebral
RT   cavernous malformations complex.";
RL   J. Cell Biol. 199:39-48(2012).
CC   -!- FUNCTION: Receptor component of the CCM signaling pathway which is
CC       a crucial regulator of heart and vessel formation and integrity
CC       May act through the stabilization of endothelial cell junctions.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CCM2 and KRIT1; KRIT1 markedly facilitates
CC       interaction with CCM2. {ECO:0000269|PubMed:23007647}.
CC   -!- INTERACTION:
CC       O00522:KRIT1; NbExp=5; IntAct=EBI-12734419, EBI-1573121;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305};
CC       Single-pass type I membrane protein {ECO:0000305}. Cell junction
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ULI3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ULI3-2; Sequence=VSP_025275, VSP_025276;
CC         Note=No experimental confirmation available.;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH67235.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAC11336.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AC026342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB033063; BAA86551.2; -; mRNA.
DR   EMBL; AK074987; BAC11336.1; ALT_INIT; mRNA.
DR   EMBL; BC004539; AAH04539.2; -; mRNA.
DR   EMBL; BC067235; AAH67235.1; ALT_INIT; mRNA.
DR   CCDS; CCDS46898.1; -. [Q9ULI3-1]
DR   RefSeq; NP_065784.1; NM_020733.1. [Q9ULI3-1]
DR   UniGene; Hs.477420; -.
DR   PDB; 3U7D; X-ray; 2.49 A; B/D=1356-1381.
DR   PDB; 4HDQ; X-ray; 1.95 A; C=1356-1381.
DR   PDBsum; 3U7D; -.
DR   PDBsum; 4HDQ; -.
DR   ProteinModelPortal; Q9ULI3; -.
DR   SMR; Q9ULI3; -.
DR   BioGrid; 121560; 3.
DR   CORUM; Q9ULI3; -.
DR   IntAct; Q9ULI3; 1.
DR   STRING; 9606.ENSP00000311502; -.
DR   GlyConnect; 763; -.
DR   iPTMnet; Q9ULI3; -.
DR   PhosphoSitePlus; Q9ULI3; -.
DR   SwissPalm; Q9ULI3; -.
DR   UniCarbKB; Q9ULI3; -.
DR   BioMuta; HEG1; -.
DR   DMDM; 147645934; -.
DR   EPD; Q9ULI3; -.
DR   jPOST; Q9ULI3; -.
DR   PaxDb; Q9ULI3; -.
DR   PeptideAtlas; Q9ULI3; -.
DR   PRIDE; Q9ULI3; -.
DR   ProteomicsDB; 85037; -.
DR   ProteomicsDB; 85038; -. [Q9ULI3-2]
DR   Ensembl; ENST00000311127; ENSP00000311502; ENSG00000173706. [Q9ULI3-1]
DR   GeneID; 57493; -.
DR   KEGG; hsa:57493; -.
DR   UCSC; uc003ehs.4; human. [Q9ULI3-1]
DR   CTD; 57493; -.
DR   DisGeNET; 57493; -.
DR   EuPathDB; HostDB:ENSG00000173706.12; -.
DR   GeneCards; HEG1; -.
DR   H-InvDB; HIX0003945; -.
DR   HGNC; HGNC:29227; HEG1.
DR   HPA; HPA010952; -.
DR   HPA; HPA011559; -.
DR   MIM; 614182; gene.
DR   neXtProt; NX_Q9ULI3; -.
DR   OpenTargets; ENSG00000173706; -.
DR   PharmGKB; PA142671699; -.
DR   eggNOG; ENOG410IJZT; Eukaryota.
DR   eggNOG; ENOG410Y1MK; LUCA.
DR   GeneTree; ENSGT00710000106813; -.
DR   HOGENOM; HOG000112879; -.
DR   InParanoid; Q9ULI3; -.
DR   OMA; GERSITG; -.
DR   OrthoDB; 236256at2759; -.
DR   PhylomeDB; Q9ULI3; -.
DR   TreeFam; TF335941; -.
DR   ChiTaRS; HEG1; human.
DR   GenomeRNAi; 57493; -.
DR   PRO; PR:Q9ULI3; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000173706; Expressed in 245 organ(s), highest expression level in parietal pleura.
DR   ExpressionAtlas; Q9ULI3; baseline and differential.
DR   Genevisible; Q9ULI3; HS.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003209; P:cardiac atrium morphogenesis; IEA:Ensembl.
DR   GO; GO:0055017; P:cardiac muscle tissue growth; IEA:Ensembl.
DR   GO; GO:0007043; P:cell-cell junction assembly; IEA:InterPro.
DR   GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0003017; P:lymph circulation; IEA:Ensembl.
DR   GO; GO:0001945; P:lymph vessel development; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:1905709; P:negative regulation of membrane permeability; IDA:UniProtKB.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR   GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0060039; P:pericardium development; IEA:Ensembl.
DR   GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:1902414; P:protein localization to cell junction; IMP:UniProtKB.
DR   GO; GO:0050878; P:regulation of body fluid levels; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   GO; GO:0048845; P:venous blood vessel morphogenesis; IEA:Ensembl.
DR   GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR   GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR028720; HEG.
DR   PANTHER; PTHR24037; PTHR24037; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell junction;
KW   Cell membrane; Complete proteome; Developmental protein;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   CHAIN        30   1381       Protein HEG homolog 1.
FT                                /FTId=PRO_0000286981.
FT   TOPO_DOM     30   1248       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1249   1269       Helical. {ECO:0000255}.
FT   TOPO_DOM   1270   1381       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      985   1023       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1025   1063       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   COMPBIAS    463    743       Ser-rich.
FT   MOD_RES    1359   1359       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:E9Q7X6}.
FT   CARBOHYD     67     67       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:22171320}.
FT   CARBOHYD    123    123       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    159    159       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    180    180       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    314    314       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    462    462       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    520    520       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    610    610       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1137   1137       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    989   1000       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    994   1011       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1013   1022       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1029   1040       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1034   1049       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1051   1062       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     986   1012       VNSCAVNPCLHNGECVADNTSRGYHCR -> GKTQSHKHML
FT                                TARPSPALRATWGSGFM (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_025275.
FT   VAR_SEQ    1013   1381       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_025276.
FT   VARIANT     145    145       Q -> R (in dbSNP:rs4404487).
FT                                /FTId=VAR_048984.
FT   VARIANT     305    305       S -> P (in dbSNP:rs2981546).
FT                                /FTId=VAR_059269.
FT   VARIANT     602    602       F -> S (in dbSNP:rs6790837).
FT                                /FTId=VAR_032253.
FT   VARIANT     980    980       V -> L (in dbSNP:rs10804567).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_032254.
FT   VARIANT    1039   1039       M -> T (in dbSNP:rs6438869).
FT                                /FTId=VAR_032255.
SQ   SEQUENCE   1381 AA;  147461 MW;  2E8402AC5227F95C CRC64;
     MASPRASRWP PPLLLLLLPL LLLPPAAPGT RDPPPSPARR ALSLAPLAGA GLELQLERRP
     EREPPPTPPR ERRGPATPGP SYRAPEPGAA TQRGPSGRAP RGGSADAAWK HWPESNTEAH
     VENITFYQNQ EDFSTVSSKE GVMVQTSGKS HAASDAPENL TLLAETADAR GRSGSSSRTN
     FTILPVGYSL EIATALTSQS GNLASESLHL PSSSSEFDER IAAFQTKSGT ASEMGTERAM
     GLSEEWTVHS QEATTSAWSP SFLPALEMGE LTTPSRKRNS SGPDLSWLHF YRTAASSPLL
     DLSSSSESTE KLNNSTGLQS SSVSQTKTMH VATVFTDGGP RTLRSLTVSL GPVSKTEGFP
     KDSRIATTSS SVLLSPSAVE SRRNSRVTGN PGDEEFIEPS TENEFGLTSL RWQNDSPTFG
     EHQLASSSEV QNGSPMSQTE TVSRSVAPMR GGEITAHWLL TNSTTSADVT GSSASYPEGV
     NASVLTQFSD STVQSGGSHT ALGDRSYSES SSTSSSESLN SSAPRGERSI AGISYGQVRG
     TAIEQRTSSD HTDHTYLSST FTKGERALLS ITDNSSSSDI VESSTSYIKI SNSSHSEYSS
     FFHAQTERSN ISSYDGEYAQ PSTESPVLHT SNLPSYTPTI NMPNTSVVLD TDAEFVSDSS
     SSSSSSSSSS SSGPPLPLPS VSQSHHLFSS ILPSTRASVH LLKSTSDAST PWSSSPSPLP
     VSLTTSTSAP LSVSQTTLPQ SSSTPVLPRA RETPVTSFQT STMTSFMTML HSSQTADLKS
     QSTPHQEKVI TESKSPSLVS LPTESTKAVT TNSPLPPSLT ESSTEQTLPA TSTNLAQMSP
     TFTTTILKTS QPLMTTPGTL SSTASLVTGP IAVQTTAGKQ LSLTHPEILV PQISTEGGIS
     TERNRVIVDA TTGLIPLTSV PTSAKEMTTK LGVTAEYSPA SRSLGTSPSP QTTVVSTAED
     LAPKSATFAV QSSTQSPTTV SSSASVNSCA VNPCLHNGEC VADNTSRGYH CRCPPSWQGD
     DCSVDVNECL SNPCPSTAMC NNTQGSFICK CPVGYQLEKG ICNLVRTFVT EFKLKRTFLN
     TTVEKHSDLQ EVENEITKTL NMCFSALPSY IRSTVHASRE SNAVVISLQT TFSLASNVTL
     FDLADRMQKC VNSCKSSAEV CQLLGSQRRI FRAGSLCKRK SPECDKDTSI CTDLDGVALC
     QCKSGYFQFN KMDHSCRACE DGYRLENETC MSCPFGLGGL NCGNPYQLIT VVIAAAGGGL
     LLILGIALIV TCCRKNKNDI SKLIFKSGDF QMSPYAEYPK NPRSQEWGRE AIEMHENGST
     KNLLQMTDVY YSPTSVRNPE LERNGLYPAY TGLPGSRHSC IFPGQYNPSF ISDESRRRDY
     F
//
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