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GNAI3_RAT
ID   GNAI3_RAT               Reviewed;         354 AA.
AC   P08753;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 193.
DE   RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-3;
DE   AltName: Full=G(i) alpha-3;
GN   Name=Gnai3; Synonyms=Gnai-3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2834384; DOI=10.1016/s0021-9258(18)68692-2;
RA   Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.;
RT   "Presence of three distinct molecular species of Gi protein alpha subunit.
RT   Structure of rat cDNAs and human genomic DNAs.";
RL   J. Biol. Chem. 263:6656-6664(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=2820999; DOI=10.1016/s0021-9258(18)47929-x;
RA   Jones D.T., Reed R.R.;
RT   "Molecular cloning of five GTP-binding protein cDNA species from rat
RT   olfactory neuroepithelium.";
RL   J. Biol. Chem. 262:14241-14249(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 111-125, FUNCTION, AND SUBUNIT.
RX   PubMed=2159473; DOI=10.1016/s0021-9258(19)39064-7;
RA   Linder M.E., Ewald D.A., Miller R.J., Gilman A.G.;
RT   "Purification and characterization of Go alpha and three types of Gi alpha
RT   after expression in Escherichia coli.";
RL   J. Biol. Chem. 265:8243-8251(1990).
RN   [4]
RP   INTERACTION WITH GPSM1.
RX   PubMed=11121039; DOI=10.1073/pnas.97.26.14364;
RA   de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B.,
RA   Siderovski D.P., Farquhar M.G.;
RT   "Activator of G protein signaling 3 is a guanine dissociation inhibitor for
RT   Galpha i subunits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000).
RN   [5]
RP   INTERACTION WITH RGS12 AND RGS14.
RX   PubMed=11387333; DOI=10.1074/jbc.m103208200;
RA   Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A.,
RA   Gist Farquhar M., Siderovski D.P.;
RT   "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
RT   guanine nucleotide dissociation inhibitor activity.";
RL   J. Biol. Chem. 276:29275-29281(2001).
RN   [6]
RP   INTERACTION WITH RGS14.
RX   PubMed=16870394; DOI=10.1016/j.cellsig.2006.06.002;
RA   Shu F.J., Ramineni S., Amyot W., Hepler J.R.;
RT   "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR
RT   domain of RGS14 influence its dynamic subcellular localization.";
RL   Cell. Signal. 19:163-176(2007).
RN   [7]
RP   INTERACTION WITH CCDC88A, AND MUTAGENESIS OF ARG-208; TRP-211 AND PHE-215.
RX   PubMed=19211784; DOI=10.1073/pnas.0900294106;
RA   Garcia-Marcos M., Ghosh P., Farquhar M.G.;
RT   "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates
RT   Akt signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009).
RN   [8]
RP   IDENTIFICATION IN COMPLEX WITH CCDC88A AND EGFR, AND MUTAGENESIS OF GLY-203
RP   AND GLN-204.
RX   PubMed=20462955; DOI=10.1091/mbc.e10-01-0028;
RA   Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P.,
RA   Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.;
RT   "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor
RT   and determines whether cells migrate or proliferate.";
RL   Mol. Biol. Cell 21:2338-2354(2010).
RN   [9]
RP   INTERACTION WITH NUCB1 AND NUCB2, AND MUTAGENESIS OF TRP-211; PHE-215;
RP   LYS-248 AND TRP-258.
RX   PubMed=21653697; DOI=10.1074/jbc.m110.204099;
RA   Garcia-Marcos M., Kietrsunthorn P.S., Wang H., Ghosh P., Farquhar M.G.;
RT   "G Protein binding sites on Calnuc (nucleobindin 1) and NUCB2 (nucleobindin
RT   2) define a new class of G(alpha)i-regulatory motifs.";
RL   J. Biol. Chem. 286:28138-28149(2011).
RN   [10]
RP   INTERACTION WITH INSR.
RX   PubMed=25187647; DOI=10.1091/mbc.e14-05-0978;
RA   Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M.,
RA   Kufareva I., Abagyan R., Ghosh P.;
RT   "Structural basis for activation of trimeric Gi proteins by multiple growth
RT   factor receptors via GIV/Girdin.";
RL   Mol. Biol. Cell 25:3654-3671(2014).
RN   [11] {ECO:0007744|PDB:6MHF}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 26-354 IN COMPLEX WITH HUMAN
RP   CCDC88A AND WITH SYNTHETIC G-ALPHA SUBUNIT-BINDING PEPTIDE, AND MUTAGENESIS
RP   OF GLN-204; TRP-211 AND PHE-215.
RX   PubMed=31363053; DOI=10.1073/pnas.1906658116;
RA   Kalogriopoulos N.A., Rees S.D., Ngo T., Kopcho N.J., Ilatovskiy A.V.,
RA   Sun N., Komives E.A., Chang G., Ghosh P., Kufareva I.;
RT   "Structural basis for GPCR-independent activation of heterotrimeric Gi
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:16394-16403(2019).
RN   [12]
RP   ERRATUM OF PUBMED:31363053.
RX   PubMed=31570568; DOI=10.1073/pnas.1916094116;
RA   Kalogriopoulos N.A., Rees S.D., Ngo T., Kopcho N.J., Ilatovskiy A.V.,
RA   Sun N., Komives E.A., Chang G., Ghosh P., Kufareva I.;
RL   Proc. Natl. Acad. Sci. U.S.A. 116:20794-20794(2019).
CC   -!- FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G
CC       proteins) function as transducers downstream of G protein-coupled
CC       receptors (GPCRs) in numerous signaling cascades. The alpha chain
CC       contains the guanine nucleotide binding site and alternates between an
CC       active, GTP-bound state and an inactive, GDP-bound state. Signaling by
CC       an activated GPCR promotes GDP release and GTP binding. The alpha
CC       subunit has a low GTPase activity that converts bound GTP to GDP,
CC       thereby terminating the signal (PubMed:2159473). Both GDP release and
CC       GTP hydrolysis are modulated by numerous regulatory proteins. Signaling
CC       is mediated via effector proteins, such as adenylate cyclase. Inhibits
CC       adenylate cyclase activity, leading to decreased intracellular cAMP
CC       levels. Stimulates the activity of receptor-regulated K(+) channels.
CC       The active GTP-bound form prevents the association of RGS14 with
CC       centrosomes and is required for the translocation of RGS14 from the
CC       cytoplasm to the plasma membrane. May play a role in cell division.
CC       {ECO:0000250|UniProtKB:P08754, ECO:0000269|PubMed:2159473}.
CC   -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC       and gamma. The alpha subunit contains the guanine nucleotide binding
CC       site (PubMed:2159473). GTP binding causes dissociation of the
CC       heterotrimer, liberating the individual subunits so that they can
CC       interact with downstream effector proteins. Forms a complex with
CC       CCDC88A/GIV and EGFR which leads to enhanced EGFR signaling and
CC       triggering of cell migration; ligand stimulation is required for
CC       recruitment of GNAI3 to the complex (PubMed:20462955). Interacts
CC       (inactive GDP-bound form) with CCDC88A/GIV (via GBA motif); the
CC       interaction leads to activation of GNAI3 (PubMed:19211784). Interacts
CC       (inactive GDP-bound form) with CCDC88C/DAPLE (via GBA motif); the
CC       interaction leads to activation of GNAI3 (By similarity). Interacts
CC       (inactive GDP-bound form) with NUCB1 (via GBA motif) and NUCB2 (via GBA
CC       motif); the interaction leads to activation of GNAI3 (PubMed:21653697).
CC       Interacts (inactive GDP-bound form) with PLCD4 (via GBA motif); the
CC       interaction leads to activation of GNAI3 (By similarity). Interacts
CC       with INSR; the interaction is probably mediated by CCDC88A/GIV
CC       (PubMed:25187647). Interacts with GPSM1 (PubMed:11121039). Interacts
CC       (GDP-bound form) with GPSM2 (via GoLoco domains). Does not interact
CC       with RGS2. Interacts with RGS8 and RGS10; this strongly enhances the
CC       intrinsic GTPase activity (By similarity). Interacts with RGS12
CC       (PubMed:11387333). Interacts with RGS16; this strongly enhances the
CC       intrinsic GTPase activity (By similarity). Interacts (via active
CC       GTP- or inactive GDP-bound form) with RGS14 (PubMed:11387333,
CC       PubMed:16870394). {ECO:0000250|UniProtKB:P08754,
CC       ECO:0000250|UniProtKB:Q9DC51, ECO:0000269|PubMed:11121039,
CC       ECO:0000269|PubMed:11387333, ECO:0000269|PubMed:16870394,
CC       ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:20462955,
CC       ECO:0000269|PubMed:2159473, ECO:0000269|PubMed:21653697,
CC       ECO:0000269|PubMed:25187647}.
CC   -!- INTERACTION:
CC       P08753; Q5BJU7: Wasf1; NbExp=2; IntAct=EBI-874897, EBI-7269229;
CC       P08753; P49795: RGS19; Xeno; NbExp=4; IntAct=EBI-874897, EBI-874907;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell
CC       membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000305}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of
CC       interphase and mitotic cells. Detected at the cleavage furrow and/or
CC       the midbody. {ECO:0000250|UniProtKB:P08754}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:2820999}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; J03219; AAA41224.1; -; mRNA.
DR   EMBL; M20713; AAA40823.1; -; mRNA.
DR   PIR; E27423; RGRTI3.
DR   RefSeq; NP_037238.1; NM_013106.1.
DR   PDB; 6MHE; X-ray; 2.20 A; A=26-354.
DR   PDB; 6MHF; X-ray; 2.00 A; A=26-354.
DR   PDBsum; 6MHE; -.
DR   PDBsum; 6MHF; -.
DR   AlphaFoldDB; P08753; -.
DR   BMRB; P08753; -.
DR   SMR; P08753; -.
DR   BioGRID; 247672; 2.
DR   CORUM; P08753; -.
DR   DIP; DIP-608N; -.
DR   IntAct; P08753; 3.
DR   MINT; P08753; -.
DR   STRING; 10116.ENSRNOP00000026710; -.
DR   iPTMnet; P08753; -.
DR   PhosphoSitePlus; P08753; -.
DR   SwissPalm; P08753; -.
DR   jPOST; P08753; -.
DR   PaxDb; P08753; -.
DR   PRIDE; P08753; -.
DR   GeneID; 25643; -.
DR   KEGG; rno:25643; -.
DR   UCSC; RGD:2714; rat.
DR   CTD; 2773; -.
DR   RGD; 2714; Gnai3.
DR   VEuPathDB; HostDB:ENSRNOG00000019465; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   HOGENOM; CLU_014184_6_0_1; -.
DR   InParanoid; P08753; -.
DR   OMA; MRIIHDV; -.
DR   OrthoDB; 754573at2759; -.
DR   TreeFam; TF300673; -.
DR   Reactome; R-RNO-170670; Adenylate cyclase inhibitory pathway.
DR   Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR   SABIO-RK; P08753; -.
DR   PRO; PR:P08753; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000019465; Expressed in duodenum and 19 other tissues.
DR   Genevisible; P08753; RN.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0000139; C:Golgi membrane; TAS:UniProtKB.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0045121; C:membrane raft; IDA:RGD.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IPI:RGD.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0032794; F:GTPase activating protein binding; IPI:RGD.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IEP:RGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:RGD.
DR   GO; GO:0051048; P:negative regulation of secretion; TAS:UniProtKB.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR   GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IMP:RGD.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:RGD.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:RGD.
DR   GO; GO:0006906; P:vesicle fusion; IDA:RGD.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; PTHR10218; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; GTP-binding; Lipoprotein;
KW   Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW   Palmitate; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   CHAIN           2..354
FT                   /note="Guanine nucleotide-binding protein G(i) subunit
FT                   alpha-3"
FT                   /id="PRO_0000203694"
FT   DOMAIN          32..354
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          35..48
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          173..181
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          196..205
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          265..272
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          324..329
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         43..48
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         150..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         175..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         200..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         326
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         203
FT                   /note="G->A: Reduces cell migration by 50% and increases
FT                   mitosis six-fold."
FT                   /evidence="ECO:0000269|PubMed:20462955"
FT   MUTAGEN         204
FT                   /note="Q->L: No effect on promotion of cell migration or
FT                   GTP-binding activity. Increases sensitivity to activation
FT                   by CCDC88A."
FT                   /evidence="ECO:0000269|PubMed:20462955,
FT                   ECO:0000269|PubMed:31363053"
FT   MUTAGEN         208
FT                   /note="R->A: Dramatically decreases binding to CCDC88A."
FT                   /evidence="ECO:0000269|PubMed:19211784"
FT   MUTAGEN         211
FT                   /note="W->A: Abolishes binding to NUCB1. Dramatically
FT                   decreases binding to CCDC88A. Does not affect GTP-binding
FT                   activity but increases the basal exchange rate."
FT                   /evidence="ECO:0000269|PubMed:19211784,
FT                   ECO:0000269|PubMed:21653697, ECO:0000269|PubMed:31363053"
FT   MUTAGEN         215
FT                   /note="F->A: Abolishes binding to NUCB1. Dramatically
FT                   decreases binding to CCDC88A. Does not affect GTP-binding
FT                   activity but increases the basal exchange rate."
FT                   /evidence="ECO:0000269|PubMed:19211784,
FT                   ECO:0000269|PubMed:21653697, ECO:0000269|PubMed:31363053"
FT   MUTAGEN         248
FT                   /note="K->E: Abolishes binding to NUCB1."
FT                   /evidence="ECO:0000269|PubMed:21653697"
FT   MUTAGEN         248
FT                   /note="K->M: Dramatically decreases interaction with
FT                   NUCB1."
FT                   /evidence="ECO:0000269|PubMed:21653697"
FT   MUTAGEN         258
FT                   /note="W->F: No effect on interaction with NUCB1."
FT                   /evidence="ECO:0000269|PubMed:21653697"
FT   STRAND          32..40
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           63..68
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           70..91
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           100..109
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   TURN            111..116
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           134..140
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           141..145
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           152..156
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           159..162
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           171..176
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   STRAND          183..191
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   STRAND          194..201
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   STRAND          204..207
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           208..215
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   STRAND          220..226
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           227..231
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   STRAND          263..269
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           271..277
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   TURN            278..280
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           296..308
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   TURN            314..316
FT                   /evidence="ECO:0007829|PDB:6MHE"
FT   STRAND          319..323
FT                   /evidence="ECO:0007829|PDB:6MHF"
FT   HELIX           329..345
FT                   /evidence="ECO:0007829|PDB:6MHF"
SQ   SEQUENCE   354 AA;  40522 MW;  A65D63CE5A32C777 CRC64;
     MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV KQMKIIHEDG
     YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR ADDARQLFVL AGSAEEGVMT
     SELAGVIKRL WRDGGVQACF SRSREYQLND SASYYLNDLD RISQTNYIPT QQDVLRTRVK
     TTGIVETHFT FKELYFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
     NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
     AYIQCQFEDL NRRKDTKEVY THFTCATDTK NVQFVFDAVT DVIIKNNLKE CGLY
 
 
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