GenomeNet

Database: UniProt
Entry: P26012
LinkDB: P26012
Original site: P26012 
ID   ITB8_HUMAN              Reviewed;         769 AA.
AC   P26012; A4D133; B4DHD4;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   10-APR-2019, entry version 184.
DE   RecName: Full=Integrin beta-8 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ITGB8 {ECO:0000312|HGNC:HGNC:6163};
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), FUNCTION, INTERACTION WITH
RP   ITGAV, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=1918072;
RA   Moyle M., Napier M.A., McLean J.W.;
RT   "Cloning and expression of a divergent integrin subunit beta 8.";
RL   J. Biol. Chem. 266:19650-19658(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA   Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA   Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA   Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA   Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA   Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA   Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA   Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA   Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA   Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA   Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA   Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
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   FUNCTION, AND INTERACTION WITH TGFB1.
RX   PubMed=22278742; DOI=10.1091/mbc.E11-12-1018;
RA   Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.;
RT   "GARP regulates the bioavailability and activation of TGFbeta.";
RL   Mol. Biol. Cell 23:1129-1139(2012).
CC   -!- FUNCTION: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for
CC       fibronectin (PubMed:1918072). It recognizes the sequence R-G-D in
CC       its ligands (PubMed:1918072). Integrin alpha-V:beta-6
CC       (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming
CC       growth factor beta-1 (TGF-beta-1) from regulatory Latency-
CC       associated peptide (LAP), thereby playing a key role in TGF-beta-1
CC       activation on the surface of activated regulatory T-cells (Tregs)
CC       (Probable). Required during vasculogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q0VBD0, ECO:0000269|PubMed:1918072,
CC       ECO:0000305|PubMed:22278742}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit
CC       (PubMed:1918072). Beta-8 (ITGB8) associates with alpha-V (ITGAV)
CC       to form ITGAV:ITGB8 (PubMed:1918072, PubMed:22278742). ITGAV:ITGB8
CC       interacts with TGFB1 (PubMed:22278742).
CC       {ECO:0000269|PubMed:1918072, ECO:0000269|PubMed:22278742}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1918072};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P26012-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P26012-2; Sequence=VSP_056531;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Placenta, kidney, brain, ovary, uterus and in
CC       several transformed cells. Transiently expressed in 293 human
CC       embryonic kidney cells. {ECO:0000269|PubMed:1918072}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; M73780; AAA36034.1; -; mRNA.
DR   EMBL; AK295044; BAG58095.1; -; mRNA.
DR   EMBL; AC004130; AAQ96845.1; -; Genomic_DNA.
DR   EMBL; CH236948; EAL24275.1; -; Genomic_DNA.
DR   EMBL; CH471073; EAW93725.1; -; Genomic_DNA.
DR   CCDS; CCDS5370.1; -. [P26012-1]
DR   PIR; A41029; A41029.
DR   RefSeq; NP_002205.1; NM_002214.2. [P26012-1]
DR   RefSeq; XP_011513698.1; XM_011515396.1. [P26012-2]
DR   RefSeq; XP_016867667.1; XM_017012178.1. [P26012-1]
DR   RefSeq; XP_016867668.1; XM_017012179.1. [P26012-1]
DR   RefSeq; XP_016867669.1; XM_017012180.1. [P26012-2]
DR   RefSeq; XP_016867670.1; XM_017012181.1. [P26012-2]
DR   RefSeq; XP_016867671.1; XM_017012182.1. [P26012-2]
DR   RefSeq; XP_016867672.1; XM_017012183.1. [P26012-2]
DR   UniGene; Hs.592171; -.
DR   UniGene; Hs.686110; -.
DR   PDB; 6DJP; EM; 4.80 A; B=43-681.
DR   PDBsum; 6DJP; -.
DR   ProteinModelPortal; P26012; -.
DR   SMR; P26012; -.
DR   BioGrid; 109902; 14.
DR   ComplexPortal; CPX-1821; Integrin alphav-beta8 complex.
DR   CORUM; P26012; -.
DR   IntAct; P26012; 1.
DR   STRING; 9606.ENSP00000222573; -.
DR   ChEMBL; CHEMBL3430892; -.
DR   iPTMnet; P26012; -.
DR   PhosphoSitePlus; P26012; -.
DR   BioMuta; ITGB8; -.
DR   DMDM; 124975; -.
DR   EPD; P26012; -.
DR   jPOST; P26012; -.
DR   MaxQB; P26012; -.
DR   PaxDb; P26012; -.
DR   PeptideAtlas; P26012; -.
DR   PRIDE; P26012; -.
DR   ProteomicsDB; 54309; -.
DR   DNASU; 3696; -.
DR   Ensembl; ENST00000222573; ENSP00000222573; ENSG00000105855. [P26012-1]
DR   Ensembl; ENST00000537992; ENSP00000441561; ENSG00000105855. [P26012-2]
DR   GeneID; 3696; -.
DR   KEGG; hsa:3696; -.
DR   UCSC; uc003suu.4; human. [P26012-1]
DR   CTD; 3696; -.
DR   DisGeNET; 3696; -.
DR   EuPathDB; HostDB:ENSG00000105855.9; -.
DR   GeneCards; ITGB8; -.
DR   HGNC; HGNC:6163; ITGB8.
DR   HPA; HPA027796; -.
DR   HPA; HPA027797; -.
DR   MIM; 604160; gene.
DR   neXtProt; NX_P26012; -.
DR   OpenTargets; ENSG00000105855; -.
DR   PharmGKB; PA29962; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P26012; -.
DR   KO; K06591; -.
DR   OMA; SASAQHC; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P26012; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   SignaLink; P26012; -.
DR   SIGNOR; P26012; -.
DR   ChiTaRS; ITGB8; human.
DR   GeneWiki; ITGB8; -.
DR   GenomeRNAi; 3696; -.
DR   PRO; PR:P26012; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000105855; Expressed in 196 organ(s), highest expression level in pigmented layer of retina.
DR   Genevisible; P26012; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0034686; C:integrin alphav-beta8 complex; IDA:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:1990430; F:extracellular matrix protein binding; IDA:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0051216; P:cartilage development; IMP:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0001573; P:ganglioside metabolic process; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0060674; P:placenta blood vessel development; TAS:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR   GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR015442; Integrin_bsu-8.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF9; PTHR10082:SF9; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002512; Integrin_B; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM00423; PSI; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW   Complete proteome; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     42       {ECO:0000255}.
FT   CHAIN        43    769       Integrin beta-8.
FT                                /FTId=PRO_0000016354.
FT   TOPO_DOM     43    684       Extracellular. {ECO:0000255}.
FT   TRANSMEM    685    704       Helical. {ECO:0000255}.
FT   TOPO_DOM    705    769       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      146    384       VWFA.
FT   REPEAT      471    510       I.
FT   REPEAT      511    552       II.
FT   REPEAT      553    592       III.
FT   REPEAT      593    629       IV.
FT   REGION      471    629       Cysteine-rich tandem repeats.
FT   CARBOHYD    233    233       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    431    431       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    466    466       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    648    648       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47    469       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     55     65       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     58     94       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     68     83       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    211    218       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    266    307       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    407    419       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    467    471       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    481    494       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    491    520       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    526    531       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    528    561       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    533    546       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    567    572       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    574    583       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    607    612       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    609    657       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    614    624       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    627    630       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    634    643       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   VAR_SEQ       1    135       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056531.
FT   VARIANT     552    552       S -> F (in dbSNP:rs5002476).
FT                                /FTId=VAR_034028.
SQ   SEQUENCE   769 AA;  85632 MW;  F7E3994F92B12A65 CRC64;
     MCGSALAFFT AAFVCLQNDR RGPASFLWAA WVFSLVLGLG QGEDNRCASS NAASCARCLA
     LGPECGWCVQ EDFISGGSRS ERCDIVSNLI SKGCSVDSIE YPSVHVIIPT ENEINTQVTP
     GEVSIQLRPG AEANFMLKVH PLKKYPVDLY YLVDVSASMH NNIEKLNSVG NDLSRKMAFF
     SRDFRLGFGS YVDKTVSPYI SIHPERIHNQ CSDYNLDCMP PHGYIHVLSL TENITEFEKA
     VHRQKISGNI DTPEGGFDAM LQAAVCESHI GWRKEAKRLL LVMTDQTSHL ALDSKLAGIV
     VPNDGNCHLK NNVYVKSTTM EHPSLGQLSE KLIDNNINVI FAVQGKQFHW YKDLLPLLPG
     TIAGEIESKA ANLNNLVVEA YQKLISEVKV QVENQVQGIY FNITAICPDG SRKPGMEGCR
     NVTSNDEVLF NVTVTMKKCD VTGGKNYAII KPIGFNETAK IHIHRNCSCQ CEDNRGPKGK
     CVDETFLDSK CFQCDENKCH FDEDQFSSES CKSHKDQPVC SGRGVCVCGK CSCHKIKLGK
     VYGKYCEKDD FSCPYHHGNL CAGHGECEAG RCQCFSGWEG DRCQCPSAAA QHCVNSKGQV
     CSGRGTCVCG RCECTDPRSI GRFCEHCPTC YTACKENWNC MQCLHPHNLS QAILDQCKTS
     CALMEQQHYV DQTSECFSSP SYLRIFFIIF IVTFLIGLLK VLIIRQVILQ WNSNKIKSSS
     DYRVSASKKD KLILQSVCTR AVTYRREKPE EIKMDISKLN AHETFRCNF
//
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