GenomeNet

Database: UniProt
Entry: PTRO_DROME
LinkDB: PTRO_DROME
Original site: PTRO_DROME 
ID   PTRO_DROME              Reviewed;        1630 AA.
AC   A1ZAU8; A1ZAU9; A1ZAV0; Q86NU5; Q8MSU7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-JUL-2019, entry version 112.
DE   RecName: Full=Patronin;
DE   AltName: Full=Short spindle protein 4;
GN   Name=Patronin; Synonyms=l(2)k07433, ssp4; ORFNames=CG33130;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Testis;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 941-1630 (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-322; SER-422; SER-431;
RP   SER-441; SER-460; SER-463; SER-466; THR-492; SER-494; SER-496;
RP   SER-513; SER-530; SER-1034; SER-1035; SER-1036; SER-1219; SER-1228;
RP   SER-1398; SER-1399 AND SER-1400, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-1067, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
RA   Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy
RT   for (quantitative) phosphoproteomics: application to Drosophila
RT   melanogaster Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=17412918; DOI=10.1126/science.1141314;
RA   Goshima G., Wollman R., Goodwin S.S., Zhang N., Scholey J.M.,
RA   Vale R.D., Stuurman N.;
RT   "Genes required for mitotic spindle assembly in Drosophila S2 cells.";
RL   Science 316:417-421(2007).
RN   [8]
RP   FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=20946984; DOI=10.1016/j.cell.2010.09.022;
RA   Goodwin S.S., Vale R.D.;
RT   "Patronin regulates the microtubule network by protecting microtubule
RT   minus ends.";
RL   Cell 143:263-274(2010).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24100293; DOI=10.1083/jcb.201306001;
RA   Wang H., Brust-Mascher I., Civelekoglu-Scholey G., Scholey J.M.;
RT   "Patronin mediates a switch from kinesin-13-dependent poleward flux to
RT   anaphase B spindle elongation.";
RL   J. Cell Biol. 203:35-46(2013).
RN   [10]
RP   FUNCTION.
RX   PubMed=26246606; DOI=10.1091/mbc.E15-02-0113;
RA   Carvalhal S., Ribeiro S.A., Arocena M., Kasciukovic T., Temme A.,
RA   Koehler K., Huebner A., Griffis E.R.;
RT   "The nucleoporin ALADIN regulates Aurora A localization to ensure
RT   robust mitotic spindle formation.";
RL   Mol. Biol. Cell 26:3424-3438(2015).
RN   [11]
RP   FUNCTION.
RX   PubMed=26659188; DOI=10.1038/nature16443;
RA   Derivery E., Seum C., Daeden A., Loubery S., Holtzer L., Juelicher F.,
RA   Gonzalez-Gaitan M.;
RT   "Polarized endosome dynamics by spindle asymmetry during asymmetric
RT   cell division.";
RL   Nature 528:280-285(2015).
CC   -!- FUNCTION: Involved in mitotic spindle assembly (PubMed:17412918,
CC       PubMed:26246606). Regulates microtubule (MT) severing
CC       (PubMed:17412918). Antagonizes the activity of the kinesin-13
CC       depolymerase Klp10A thereby switching off the depolymerization of
CC       the MTs at their pole-associated minus ends, which turns off
CC       poleward flux and induces anaphase B spindle elongation
CC       (PubMed:20946984, PubMed:24100293). Involved in asymmetric cell
CC       division of sensory organ precursor (SOP) cells by playing a role
CC       in the asymmetric localization of Sara-expressing endosomes to the
CC       pIIa daughter cell but not to the pIIb cell. Klp98A targets Sara-
CC       expressing endosomes to the central spindle which is symmetrically
CC       arranged in early cell division. During late cytokinesis, central
CC       spindle asymmetry is generated by enrichment of Patronin on the
CC       pIIb side which protects microtubules from depolymerization by
CC       Klp10A while unprotected microtubules on the pIIa side are
CC       disassembled by Klp10A, leading to the asymmetric delivery of
CC       Sara-expressing endosomes to the pIIa daughter cell
CC       (PubMed:26659188). {ECO:0000269|PubMed:17412918,
CC       ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:24100293,
CC       ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:26659188}.
CC   -!- SUBUNIT: Associates with the minus end of the microtubules.
CC       {ECO:0000269|PubMed:20946984}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC       organizing center, spindle pole body. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome. Note=Localizes to
CC       centrosomes in prophase, to the midbody during cytokinesis,
CC       diffusely throughout the metaphase spindle and to punctae in
CC       interphase that often overlap with MTs. Colocalizes with Sas-4 and
CC       SAK at the microtubule organizing center.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=C;
CC         IsoId=A1ZAU8-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=A;
CC         IsoId=A1ZAU8-2; Sequence=VSP_037213, VSP_037214, VSP_037215;
CC         Note=No experimental confirmation available.;
CC       Name=B;
CC         IsoId=A1ZAU8-3; Sequence=VSP_037213, VSP_037214, VSP_037216;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000255|PROSITE-
CC       ProRule:PRU00841}.
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00841}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM49943.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AE013599; AAO41362.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAS64821.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAS64822.1; -; Genomic_DNA.
DR   EMBL; BT003634; AAO39638.1; -; mRNA.
DR   EMBL; AY118574; AAM49943.1; ALT_INIT; mRNA.
DR   RefSeq; NP_788398.1; NM_176218.3. [A1ZAU8-2]
DR   RefSeq; NP_995875.1; NM_206153.3. [A1ZAU8-1]
DR   RefSeq; NP_995876.1; NM_206154.3. [A1ZAU8-3]
DR   BioGrid; 62669; 19.
DR   IntAct; A1ZAU8; 4.
DR   STRING; 7227.FBpp0304550; -.
DR   iPTMnet; A1ZAU8; -.
DR   PRIDE; A1ZAU8; -.
DR   EnsemblMetazoa; FBtr0086948; FBpp0086104; FBgn0263197. [A1ZAU8-2]
DR   EnsemblMetazoa; FBtr0086949; FBpp0086105; FBgn0263197. [A1ZAU8-3]
DR   EnsemblMetazoa; FBtr0086950; FBpp0086106; FBgn0263197. [A1ZAU8-1]
DR   GeneID; 36978; -.
DR   KEGG; dme:Dmel_CG33130; -.
DR   UCSC; CG33130-RA; d. melanogaster.
DR   UCSC; CG33130-RB; d. melanogaster.
DR   UCSC; CG33130-RC; d. melanogaster. [A1ZAU8-1]
DR   CTD; 36978; -.
DR   FlyBase; FBgn0263197; Patronin.
DR   GeneTree; ENSGT00950000182975; -.
DR   InParanoid; A1ZAU8; -.
DR   KO; K17493; -.
DR   GenomeRNAi; 36978; -.
DR   PRO; PR:A1ZAU8; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0263197; Expressed in 27 organ(s), highest expression level in head.
DR   ExpressionAtlas; A1ZAU8; baseline and differential.
DR   Genevisible; A1ZAU8; DM.
DR   GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; IDA:FlyBase.
DR   GO; GO:0005819; C:spindle; IDA:FlyBase.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; ISS:FlyBase.
DR   GO; GO:0051011; F:microtubule minus-end binding; IDA:FlyBase.
DR   GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR   GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   GO; GO:0061867; P:establishment of mitotic spindle asymmetry; IMP:FlyBase.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase.
DR   GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR   Gene3D; 3.10.20.360; -; 1.
DR   InterPro; IPR032940; CAMSAP.
DR   InterPro; IPR031372; CAMSAP_CC1.
DR   InterPro; IPR022613; CAMSAP_CH.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR038209; CKK_dom_sf.
DR   InterPro; IPR014797; CKK_domain.
DR   InterPro; IPR011033; PRC_barrel-like_sf.
DR   PANTHER; PTHR21595; PTHR21595; 2.
DR   Pfam; PF17095; CAMSAP_CC1; 1.
DR   Pfam; PF11971; CAMSAP_CH; 1.
DR   Pfam; PF08683; CAMSAP_CKK; 1.
DR   SMART; SM01051; CAMSAP_CKK; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   SUPFAM; SSF50346; SSF50346; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51508; CKK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Coiled coil; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1   1630       Patronin.
FT                                /FTId=PRO_0000372861.
FT   DOMAIN      156    288       Calponin-homology (CH).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00044}.
FT   DOMAIN     1489   1623       CKK. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00841}.
FT   COILED      601    639       {ECO:0000255}.
FT   COILED     1277   1343       {ECO:0000255}.
FT   COMPBIAS    360    394       Gln-rich.
FT   COMPBIAS    671   1027       Gln-rich.
FT   MOD_RES     322    322       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     422    422       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     431    431       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     441    441       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     460    460       Phosphoserine.
FT                                {ECO:0000269|PubMed:17372656,
FT                                ECO:0000269|PubMed:18327897}.
FT   MOD_RES     463    463       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     466    466       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     492    492       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     494    494       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     496    496       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     513    513       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     530    530       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1034   1034       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1035   1035       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1036   1036       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1067   1067       Phosphoserine.
FT                                {ECO:0000269|PubMed:17372656}.
FT   MOD_RES    1219   1219       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1228   1228       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1398   1398       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1399   1399       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1400   1400       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   VAR_SEQ     418    418       R -> RGDFVAAGRPSNWEQSRRPSFA (in isoform A
FT                                and isoform B).
FT                                {ECO:0000303|PubMed:12537569,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_037213.
FT   VAR_SEQ     671    719       Missing (in isoform A and isoform B).
FT                                {ECO:0000303|PubMed:12537569,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_037214.
FT   VAR_SEQ    1404   1488       Missing (in isoform A).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_037215.
FT   VAR_SEQ    1404   1488       GYGQLSSNSMKRDYYRGSQDSLTVKESPDDYPSTSSTPIGR
FT                                RGSYKTSREPAGVERGRTLSRISVAKGSTLNFRGRKSNSLM
FT                                NLC -> DSGLGRATPPRRAPSPGMGMGAS (in
FT                                isoform B).
FT                                {ECO:0000303|PubMed:12537569}.
FT                                /FTId=VSP_037216.
FT   CONFLICT    805    805       T -> A (in Ref. 3; AAO39638).
FT                                {ECO:0000305}.
FT   CONFLICT   1170   1170       N -> S (in Ref. 3; AAO39638).
FT                                {ECO:0000305}.
FT   CONFLICT   1177   1177       P -> H (in Ref. 3; AAO39638).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1630 AA;  183622 MW;  B8182F1FCEBF51DF CRC64;
     MDVETQEIRQ ARQRASVKWL LSKAFNNRVP DNLKEPFYRD HENQERLKPQ IIVELGNATL
     YCQTLANLYS DPNYQSMNHW SIIQTLARKG VPVAESADMP ITETVLIQTN PLRINAHMSV
     IESLMVLYAK EISSGDRVMA AIRRISGNNY QAPTGQSYEQ ALLGWISHAC AALKKRIIKE
     VDAGLPDDNG SRLQTPDIPP VRDFQDLCDG ICLALLISYY CPKVVPWTSV RINYLPAVED
     SIHNILLVCN FSQKHLPYTV MHMTPEDVTY MRGSMKLNLV VLLTDLFNLF EIHPAKCVCY
     PGMDGQVPHS NSFGGGLNRR STPPNEYQTV QSNNFDGNHA EAFVVHKSRG ITTLASMHSQ
     QQQQLHQQQQ HQQQYHQQPL QQHPSQSQLQ IQQQEPLVPA RLRQAKEKTN VESKADERGR
     RSRRNSSSED SQLTIENFGG SQDQLNTLGR YERDRERKLS NTSVGSYPVE PAVAVRSSIA
     DARGTLQLGY DTDSGSEKQD RETEKYSMRR QVSVDNVPTV SSHNLSNAGS PLPVARHKQH
     SSDKDYSSNS GMTPDAYNDS RSTSGYDPES TPVRKSSTSS MPASPAAWQL DVGDDDMRSL
     ENASKLSTIR MKLEEKRRRI EQDKRKIEMA LLRHQEKEDL ESCPDVMKWE TMSNESKRTP
     DMDPVDLDKY QQSIAIMNMN LQDIQQDIHR LATQQSQMQA QHLQAQQLMQ AQQIANMLNQ
     AYNAPVSAYS SRPPSRDPYQ QQLHHQQQQP MPMPQPMQYV NEHGQYMSPP QPAHYMPQQA
     QQPQSIYSDN GAAYNHSNHS PYGGTPQYRS SVVYDDYGQP TNHFYLHESS PQPQAHQHPQ
     RRTWAHSAAA AAYEQQQQIQ PSLVDVNAWQ TQQHQKQKQT WMNRPPSSAG APSPGSFMLH
     QNGGGGGGGG GGGELQHLFQ VQASPQHGQR QVSGSNGVQR QQSLTNLRDN RSPKAPQNMG
     MPMGMPMQQE DMMAPQSICF IGDEEDVDEL ERNIIESMQS THISDFVHQQ QQQHQHQQQL
     QQQQRLQGHS GRGSSSEDYD SGEMISNKLN ITSGNLTYRI PSPSRPSIQA NSFQDPRAMA
     AASGGEDQPP EKGFYISFDD EQPKRPKPPL RAKRSPKKES PPGSRDSVDN QATLKRESLS
     HLHNNNNIGF GNDDVNSKPV TRHSIHGLNN SNSVKSPGNA TYNKYTDEPP IQLRQLAVSG
     AMSPTSNERH HLDDVSNQSP QQTQQPMSPT RLQQSSNNAE AAKNKALVIG ADSTNLDPES
     VDEMERRKEK IMLLSLQRRQ QQEEAKARKE IEASQKREKE REKEEERARK KEEQMARRAA
     ILEQHRLKKA IEEAEREGKT LDRPDLHVKL QSHSSTSTTP RLRQQRTTRP RPKTIHVDDA
     SVDISEASSI SSRGKKGSSS NLTGYGQLSS NSMKRDYYRG SQDSLTVKES PDDYPSTSST
     PIGRRGSYKT SREPAGVERG RTLSRISVAK GSTLNFRGRK SNSLMNLCGP KLYKQPAAKS
     NRGIILNAVE YCVFPGVVNR EAKQKVLEKI ARSEAKHFLV LFRDAGCQFR ALYSYQPETD
     QVTKLYGTGP SQVEEVMFDK FFKYNSGGKC FSQVHTKHLT VTIDAFTIHN SLWQGKRVQL
     PSKKDMALVI
//
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