GenomeNet

Database: UniProt
Entry: RHG35_RAT
LinkDB: RHG35_RAT
Original site: RHG35_RAT 
ID   RHG35_RAT               Reviewed;        1499 AA.
AC   P81128; A0A0G2KB46;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 3.
DT   18-SEP-2019, entry version 150.
DE   RecName: Full=Rho GTPase-activating protein 35 {ECO:0000312|RGD:1308738};
DE   AltName: Full=GAP-associated protein p190;
DE   AltName: Full=Glucocorticoid receptor DNA-binding factor 1;
GN   Name=Arhgap35 {ECO:0000312|RGD:1308738};
GN   Synonyms=Grlf1, P190A {ECO:0000303|PubMed:9852136},
GN   p190ARHOGAP {ECO:0000303|PubMed:9852136};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 379-391;
RP   491-506 AND 1304-1322, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=1581965; DOI=10.1016/0092-8674(92)90454-k;
RA   Settleman J., Narasimhan V., Foster L.C., Weinberg R.A.;
RT   "Molecular cloning of cDNAs encoding the GAP-associated protein p190:
RT   implications for a signaling pathway from ras to the nucleus.";
RL   Cell 69:539-549(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
RP   FUNCTION, GTP-BINDING, AND MUTAGENESIS OF SER-36 AND ARG-1284.
RX   PubMed=9852136; DOI=10.1074/jbc.273.51.34631;
RA   Tatsis N., Lannigan D.A., Macara I.G.;
RT   "The function of the p190 Rho GTPase-activating protein is controlled
RT   by its N-terminal GTP binding domain.";
RL   J. Biol. Chem. 273:34631-34638(1998).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF SER-1451 AND 1476-SER--SER-1483, AND
RP   PHOSPHORYLATION.
RX   PubMed=20439493; DOI=10.1128/mcb.01178-09;
RA   Pullikuth A.K., Catling A.D.;
RT   "Extracellular signal-regulated kinase promotes Rho-dependent focal
RT   adhesion formation by suppressing p190A RhoGAP.";
RL   Mol. Cell. Biol. 30:3233-3248(2010).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-975; SER-985;
RP   SER-1134 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Rho GTPase-activating protein (GAP). Binds several
CC       acidic phospholipids which inhibits the Rho GAP activity to
CC       promote the Rac GAP activity (PubMed:9852136, PubMed:20439493).
CC       This binding is inhibited by phosphorylation by PRKCA (By
CC       similarity). Involved in cell differentiation as well as cell
CC       adhesion and migration, plays an important role in retinal tissue
CC       morphogenesis, neural tube fusion, midline fusion of the cerebral
CC       hemispheres and mammary gland branching morphogenesis
CC       (PubMed:9852136, PubMed:20439493). Transduces signals from p21-ras
CC       to the nucleus, acting via the ras GTPase-activating protein (GAP)
CC       (By similarity). Transduces SRC-dependent signals from cell-
CC       surface adhesion molecules, such as laminin, to promote neurite
CC       outgrowth. Regulates axon outgrowth, guidance and fasciculation
CC       (By similarity). Modulates Rho GTPase-dependent F-actin
CC       polymerization, organization and assembly, is involved in
CC       polarized cell migration and in the positive regulation of
CC       ciliogenesis and cilia elongation (By similarity). During mammary
CC       gland development, is required in both the epithelial and stromal
CC       compartments for ductal outgrowth (By similarity). Represses
CC       transcription of the glucocorticoid receptor by binding to the
CC       cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this
CC       function is however unclear and would need additional experimental
CC       evidences (By similarity). {ECO:0000250|UniProtKB:Q91YM2,
CC       ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:20439493,
CC       ECO:0000269|PubMed:9852136}.
CC   -!- SUBUNIT: Interacts with RASA1 (By similarity). Interacts with the
CC       general transcription factor GTF2I, the interaction sequesters
CC       GTF2I in the cytoplasm (By similarity).
CC       {ECO:0000250|UniProtKB:Q91YM2, ECO:0000250|UniProtKB:Q9NRY4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:Q91YM2}. Cytoplasm
CC       {ECO:0000269|PubMed:1581965}. Nucleus
CC       {ECO:0000269|PubMed:1581965}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q91YM2}. Note=In response to integrins and
CC       SDC4 and upon phosphorylation by PKC, relocalizes from the
CC       cytoplasm to regions of plasma membrane ruffling where it
CC       colocalizes with polymerized actin.
CC       {ECO:0000250|UniProtKB:Q91YM2}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DOMAIN: N-terminal part (1-266) has GTPase activity. Required for
CC       proper cellular localization. {ECO:0000250|UniProtKB:Q91YM2}.
CC   -!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
CC       {ECO:0000250|UniProtKB:Q6NU25}.
CC   -!- PTM: Phosphorylation of Tyr-1105 by PTK6 promotes the association
CC       with RASA1, inactivating RHOA while activating RAS.
CC       Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I (By
CC       similarity). Phosphorylated by PRKCA at Ser-1221 and Thr-1226,
CC       induces relocalization from the cytoplasm to regions of plasma
CC       membrane ruffling and prevents the binding and substrate
CC       specificity regulation by phospholipids (By similarity). In brain,
CC       phosphorylated by FYN and SRC (By similarity). During focal
CC       adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-
CC       terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-
CC       1483. Phosphorylation by MAPK1 and MAPK3 inhibits GAP function and
CC       localizes ARGHAP35 away from newly forming focal adhesions and
CC       stress fibers in cells spreading on fibronectin (PubMed:20439493).
CC       Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming
CC       by MAPK and inhibits RhoGAP activity and modulates polarized cell
CC       migration (By similarity). {ECO:0000250|UniProtKB:Q91YM2,
CC       ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:20439493}.
DR   EMBL; M94721; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AABR07002647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07002648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A38218; A38218.
DR   RefSeq; NP_001258061.1; NM_001271132.1.
DR   RefSeq; XP_006228474.1; XM_006228412.3.
DR   RefSeq; XP_008757141.1; XM_008758919.1.
DR   PDB; 5IRC; X-ray; 1.72 A; A/B=1242-1439.
DR   PDB; 6D4G; X-ray; 2.80 A; A/B=1-266.
DR   PDBsum; 5IRC; -.
DR   PDBsum; 6D4G; -.
DR   SMR; P81128; -.
DR   STRING; 10116.ENSRNOP00000021223; -.
DR   iPTMnet; P81128; -.
DR   PhosphoSitePlus; P81128; -.
DR   jPOST; P81128; -.
DR   PaxDb; P81128; -.
DR   PRIDE; P81128; -.
DR   Ensembl; ENSRNOT00000090519; ENSRNOP00000075649; ENSRNOG00000015852.
DR   GeneID; 306400; -.
DR   KEGG; rno:306400; -.
DR   UCSC; RGD:1308738; rat.
DR   CTD; 2909; -.
DR   RGD; 1308738; Arhgap35.
DR   eggNOG; KOG4271; Eukaryota.
DR   eggNOG; ENOG410XR4E; LUCA.
DR   GeneTree; ENSGT00950000182819; -.
DR   InParanoid; P81128; -.
DR   KO; K05732; -.
DR   OrthoDB; 110157at2759; -.
DR   PhylomeDB; P81128; -.
DR   Reactome; R-RNO-194840; Rho GTPase cycle.
DR   Reactome; R-RNO-416550; Sema4D mediated inhibition of cell attachment and migration.
DR   Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR   PRO; PR:P81128; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015852; Expressed in 10 organ(s), highest expression level in brain.
DR   ExpressionAtlas; P81128; baseline and differential.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0032794; F:GTPase activating protein binding; IPI:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; ISS:UniProtKB.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:UniProtKB.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB.
DR   GO; GO:0030879; P:mammary gland development; ISS:UniProtKB.
DR   GO; GO:0097485; P:neuron projection guidance; ISS:UniProtKB.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0008064; P:regulation of actin polymerization or depolymerization; ISS:UniProtKB.
DR   GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR   Gene3D; 1.10.10.440; -; 2.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR036517; FF_domain_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039007; pG1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR032835; RhoGAP-FF1.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR039006; RhoGAP_pG2.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF01846; FF; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF16512; RhoGAP-FF1; 1.
DR   SMART; SM00441; FF; 4.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81698; SSF81698; 1.
DR   PROSITE; PS51676; FF; 4.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cell projection; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA-binding;
KW   GTP-binding; GTPase activation; Lipid-binding; Membrane;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation.
FT   CHAIN         1   1499       Rho GTPase-activating protein 35.
FT                                /FTId=PRO_0000056732.
FT   DOMAIN      270    327       FF 1.
FT   DOMAIN      368    422       FF 2.
FT   DOMAIN      429    483       FF 3.
FT   DOMAIN      485    550       FF 4.
FT   DOMAIN      592    767       pG1 pseudoGTPase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01199}.
FT   DOMAIN      783    947       pG2 pseudoGTPase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01200}.
FT   DOMAIN     1249   1436       Rho-GAP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00172}.
FT   NP_BIND      33     37       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   NP_BIND      95     97       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   NP_BIND     201    203       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   NP_BIND     229    231       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   REGION        1    266       Has GTPase activity, required for proper
FT                                localization.
FT                                {ECO:0000250|UniProtKB:Q91YM2}.
FT   REGION     1213   1236       Required for phospholipid binding and
FT                                regulation of the substrate preference.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   BINDING      28     28       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   BINDING      52     52       GTP; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   BINDING      56     56       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     308    308       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     589    589       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     770    770       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     773    773       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     970    970       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     975    975       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     985    985       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1072   1072       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1087   1087       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1105   1105       Phosphotyrosine; by ABL2 and PTK6.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1134   1134       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1142   1142       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q91YM2}.
FT   MOD_RES    1150   1150       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1176   1176       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1179   1179       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1221   1221       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1226   1226       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1236   1236       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1472   1472       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q91YM2}.
FT   MOD_RES    1476   1476       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q91YM2}.
FT   MOD_RES    1480   1480       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q91YM2}.
FT   MOD_RES    1483   1483       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q91YM2}.
FT   MUTAGEN      36     36       S->N: Disrupts GTP-binding. No direct
FT                                effect on GAP activity 'in vitro' but
FT                                affects the activity regulation 'in
FT                                vivo'. {ECO:0000269|PubMed:9852136}.
FT   MUTAGEN    1284   1284       R->A: Abolishes GAP activity.
FT                                {ECO:0000269|PubMed:9852136}.
FT   MUTAGEN    1451   1451       S->A: Abolishes phosphorylation by MAPK,
FT                                increases functional activity and
FT                                enhances retention in peripheral
FT                                membranes; when associated with 1476-A--
FT                                A-1483. {ECO:0000269|PubMed:20439493}.
FT   MUTAGEN    1476   1483       SPPPTPQS->APPPAPQA: Abolishes
FT                                phosphorylation by MAPK, increases
FT                                functional activity and enhances
FT                                retention in peripheral membranes; when
FT                                associated with A-1451.
FT                                {ECO:0000269|PubMed:20439493}.
FT   STRAND       15     19       {ECO:0000244|PDB:6D4G}.
FT   TURN         25     30       {ECO:0000244|PDB:6D4G}.
FT   HELIX        35     43       {ECO:0000244|PDB:6D4G}.
FT   TURN         47     49       {ECO:0000244|PDB:6D4G}.
FT   HELIX        60     63       {ECO:0000244|PDB:6D4G}.
FT   TURN         66     70       {ECO:0000244|PDB:6D4G}.
FT   STRAND       72     79       {ECO:0000244|PDB:6D4G}.
FT   STRAND       91     96       {ECO:0000244|PDB:6D4G}.
FT   TURN        102    104       {ECO:0000244|PDB:6D4G}.
FT   HELIX       116    120       {ECO:0000244|PDB:6D4G}.
FT   STRAND      123    126       {ECO:0000244|PDB:6D4G}.
FT   HELIX       136    138       {ECO:0000244|PDB:6D4G}.
FT   HELIX       142    144       {ECO:0000244|PDB:6D4G}.
FT   HELIX       151    153       {ECO:0000244|PDB:6D4G}.
FT   STRAND      154    156       {ECO:0000244|PDB:6D4G}.
FT   STRAND      159    165       {ECO:0000244|PDB:6D4G}.
FT   TURN        169    171       {ECO:0000244|PDB:6D4G}.
FT   HELIX       174    190       {ECO:0000244|PDB:6D4G}.
FT   STRAND      195    200       {ECO:0000244|PDB:6D4G}.
FT   HELIX       202    204       {ECO:0000244|PDB:6D4G}.
FT   HELIX       207    218       {ECO:0000244|PDB:6D4G}.
FT   STRAND      224    227       {ECO:0000244|PDB:6D4G}.
FT   TURN        230    233       {ECO:0000244|PDB:6D4G}.
FT   HELIX       236    251       {ECO:0000244|PDB:6D4G}.
FT   STRAND     1245   1249       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1251   1254       {ECO:0000244|PDB:5IRC}.
FT   STRAND     1257   1259       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1263   1275       {ECO:0000244|PDB:5IRC}.
FT   TURN       1280   1284       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1289   1301       {ECO:0000244|PDB:5IRC}.
FT   TURN       1307   1309       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1314   1327       {ECO:0000244|PDB:5IRC}.
FT   STRAND     1328   1330       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1335   1345       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1350   1361       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1366   1383       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1386   1389       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1393   1398       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1401   1405       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1412   1416       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1419   1430       {ECO:0000244|PDB:5IRC}.
FT   HELIX      1432   1436       {ECO:0000244|PDB:5IRC}.
SQ   SEQUENCE   1499 AA;  170480 MW;  B3AEBD920E98B310 CRC64;
     MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
     SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
     AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF
     VSNLYNQLAK TKKPIVIVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
     STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKSHNE NWLSVSRKMQ
     ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEVDH
     LSCIKAKKLL ETKPEFLKWF VVLEETPWDE TSHIDNMENE RIPFDLMDTV PAEQLYETHL
     EKLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
     QKQIIDRAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER
     DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL
     VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG
     CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ
     GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV
     DLRIVMCLMC GDPFSADDIL SPVLQSQTCK SSHCGSSNSV LLELPIGVHK KRIELSVLSY
     HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
     SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LELFHPFFKD VVEKKNIIEA THMYDNVAEA
     CSTTEEVFNS PRAGSPLCNS NLQDSEEDVE PPSYHLFRED ATLPSLSKDH SKFSMELEGN
     DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF EITKDLSYLD QGHREGQRKS MSSSPWMPQD
     GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT
     SSLERGRKVS AVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
     DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP
     IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA
     MKSFFSELPD PLVPYSMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN
     RVSHNNKVNL MTSENLSICF WPTLMRPDFS SMDALTATRS YQTIIELFIQ QCPFFFYNRP
     ISEPPGAAPG SPSAMAPTVP FLTSTPATSQ PSPPQSPPPT PQSPMQPLLS SQLQAEHTL
//
DBGET integrated database retrieval system