ID   GNA13_MOUSE             Reviewed;         377 AA.
AC   P27601; Q6PF99;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   24-JAN-2024, entry version 199.
DE   RecName: Full=Guanine nucleotide-binding protein subunit alpha-13;
DE            Short=G alpha-13;
DE            Short=G-protein subunit alpha-13;
GN   Name=Gna13; Synonyms=Gna-13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1905812; DOI=10.1073/pnas.88.13.5582;
RA   Strathmann M.P., Simon M.I.;
RT   "G alpha 12 and G alpha 13 subunits define a fourth class of G protein
RT   alpha subunits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5582-5586(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 51-61 AND 220-227, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 228-288.
RX   PubMed=2508088; DOI=10.1073/pnas.86.19.7407;
RA   Strathmann M., Wilkie T.M., Simon M.I.;
RT   "Diversity of the G-protein family: sequences from five additional alpha
RT   subunits in the mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989).
RN   [5]
RP   INTERACTION WITH CTNND1.
RX   PubMed=15240885; DOI=10.1073/pnas.0401366101;
RA   Krakstad B.F., Ardawatia V.V., Aragay A.M.;
RT   "A role for Galpha12/Galpha13 in p120ctn regulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:10314-10319(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=18703424; DOI=10.1095/biolreprod.107.067504;
RA   Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z.,
RA   Sha J.;
RT   "RGS22, a novel testis-specific regulator of G-protein signaling involved
RT   in human and mouse spermiogenesis along with GNA12/13 subunits.";
RL   Biol. Reprod. 79:1021-1029(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=19151758; DOI=10.1038/onc.2008.488;
RA   Lee S.J., Yang J.W., Cho I.J., Kim W.D., Cho M.K., Lee C.H., Kim S.G.;
RT   "The gep oncogenes, Galpha(12) and Galpha(13), upregulate the transforming
RT   growth factor-beta1 gene.";
RL   Oncogene 28:1230-1240(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION.
RX   PubMed=21212405; DOI=10.1161/atvbaha.110.218552;
RA   Kim Y.M., Lim S.C., Han C.Y., Kay H.Y., Cho I.J., Ki S.H., Lee M.Y.,
RA   Kwon H.M., Lee C.H., Kim S.G.;
RT   "G(alpha)12/13 induction of CYR61 in association with arteriosclerotic
RT   intimal hyperplasia: effect of sphingosine-1-phosphate.";
RL   Arterioscler. Thromb. Vasc. Biol. 31:861-869(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 47-377 IN COMPLEX WITH GTP
RP   ANALOG, FUNCTION, SUBUNIT, AND INTERACTION WITH ARHGEF1 AND ARHGEF12.
RX   PubMed=16388592; DOI=10.1021/bi051729t;
RA   Kreutz B., Yau D.M., Nance M.R., Tanabe S., Tesmer J.J., Kozasa T.;
RT   "A new approach to producing functional G alpha subunits yields the
RT   activated and deactivated structures of G alpha(12/13) proteins.";
RL   Biochemistry 45:167-174(2006).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 41-377 IN COMPLEX WITH MAGNESIUM,
RP   AND INTERACTION WITH ARHGEF11.
RX   PubMed=18940608; DOI=10.1016/j.str.2008.07.009;
RA   Chen Z., Singer W.D., Danesh S.M., Sternweis P.C., Sprang S.R.;
RT   "Recognition of the activated states of Galpha13 by the rgRGS domain of
RT   PDZRhoGEF.";
RL   Structure 16:1532-1543(2008).
RN   [12]
RP   INTERACTION WITH GAS2L2.
RX   PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA   Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT   "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT   of the A2A adenosine receptor.";
RL   Biochim. Biophys. Acta 1833:3145-3154(2013).
RN   [13]
RP   INTERACTION WITH GPR174.
RX   PubMed=31875850; DOI=10.1038/s41586-019-1873-0;
RA   Zhao R., Chen X., Ma W., Zhang J., Guo J., Zhong X., Yao J., Sun J.,
RA   Rubinfien J., Zhou X., Wang J., Qi H.;
RT   "A GPR174-CCL21 module imparts sexual dimorphism to humoral immunity.";
RL   Nature 577:416-420(2020).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling systems
CC       (PubMed:21212405, PubMed:19151758, PubMed:16388592). Activates effector
CC       molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF,
CC       ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) (PubMed:16388592). GNA13-
CC       dependent Rho signaling subsequently regulates transcription factor AP-
CC       1 (activating protein-1) (PubMed:19151758, PubMed:21212405). Promotes
CC       tumor cell invasion and metastasis by activating Rho/ROCK signaling
CC       pathway (By similarity). Inhibits CDH1-mediated cell adhesion in
CC       process independent from Rho activation (By similarity).
CC       {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:16388592,
CC       ECO:0000269|PubMed:19151758, ECO:0000269|PubMed:21212405}.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma
CC       (PubMed:16388592). The alpha chain contains the guanine nucleotide
CC       binding site (PubMed:16388592). Interacts with UBXD5 (By similarity).
CC       Interacts with HAX1 (By similarity). Interacts (in GTP-bound form) with
CC       PPP5C (via TPR repeats); activates PPP5C phosphatase activity and
CC       translocates PPP5C to the cell membrane (By similarity). Interacts with
CC       RGS22 (By similarity). Interacts (in GTP-bound form) with ARHGEF1
CC       (PubMed:16388592). Interacts (in GTP-bound form) with ARHGEF11 (via RGS
CC       domain) (PubMed:18940608). Interacts (in GTP-bound form) with ARHGEF12
CC       (via RGS domain) (PubMed:16388592). Interacts with CTNND1
CC       (PubMed:15240885). Interacts with GAS2L2 (PubMed:23994616). Interacts
CC       with GPR35 (By similarity). Interacts with GPR174 (PubMed:31875850).
CC       {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:15240885,
CC       ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:18940608,
CC       ECO:0000269|PubMed:23994616, ECO:0000269|PubMed:31875850}.
CC   -!- INTERACTION:
CC       P27601; O08915: Aip; NbExp=3; IntAct=EBI-2255627, EBI-6935014;
CC       P27601; Q9ES67: Arhgef11; Xeno; NbExp=3; IntAct=EBI-2255627, EBI-15735216;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18703424}; Lipid-
CC       anchor {ECO:0000269|PubMed:18703424}. Melanosome {ECO:0000250}.
CC       Cytoplasm {ECO:0000269|PubMed:18703424}. Nucleus
CC       {ECO:0000269|PubMed:18703424}. Note=Cytoplasmic in adult somatic cells,
CC       but mainly nuclear in spermatids in the testes. Translocates from the
CC       cytoplasm to the nucleus during spermatogenesis, hence predominantly
CC       observed in the cytoplasm of round spermatids but localized in the
CC       nuclei of elongating or elongated spermatids and testicular
CC       spermatozoa.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis, as well as in kidney
CC       and sperm (at protein level). {ECO:0000269|PubMed:18703424}.
CC   -!- PTM: Phosphorylation on Thr-203 destabilizes the heterotrimer of alpha,
CC       beta and gamma, and inhibits Rho activation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(12) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M63660; AAA37649.1; -; mRNA.
DR   EMBL; BC057665; AAH57665.1; -; mRNA.
DR   EMBL; M57620; AAA63303.1; -; mRNA.
DR   CCDS; CCDS25577.1; -.
DR   PIR; B41095; B41095.
DR   RefSeq; NP_034433.3; NM_010303.3.
DR   PDB; 1SHZ; X-ray; 2.85 A; A/D=52-159, A/D=333-376.
DR   PDB; 1ZCB; X-ray; 2.00 A; A=47-377.
DR   PDB; 3AB3; X-ray; 2.40 A; A/C=47-377.
DR   PDB; 3CX6; X-ray; 2.50 A; A=41-377.
DR   PDB; 3CX7; X-ray; 2.25 A; A=41-377.
DR   PDB; 3CX8; X-ray; 2.00 A; A=41-377.
DR   PDBsum; 1SHZ; -.
DR   PDBsum; 1ZCB; -.
DR   PDBsum; 3AB3; -.
DR   PDBsum; 3CX6; -.
DR   PDBsum; 3CX7; -.
DR   PDBsum; 3CX8; -.
DR   AlphaFoldDB; P27601; -.
DR   SMR; P27601; -.
DR   BioGRID; 199963; 24.
DR   DIP; DIP-46241N; -.
DR   IntAct; P27601; 6.
DR   MINT; P27601; -.
DR   STRING; 10090.ENSMUSP00000020930; -.
DR   GlyGen; P27601; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P27601; -.
DR   PhosphoSitePlus; P27601; -.
DR   SwissPalm; P27601; -.
DR   EPD; P27601; -.
DR   jPOST; P27601; -.
DR   MaxQB; P27601; -.
DR   PaxDb; 10090-ENSMUSP00000020930; -.
DR   PeptideAtlas; P27601; -.
DR   ProteomicsDB; 267733; -.
DR   Pumba; P27601; -.
DR   Antibodypedia; 31626; 304 antibodies from 30 providers.
DR   DNASU; 14674; -.
DR   Ensembl; ENSMUST00000020930.14; ENSMUSP00000020930.8; ENSMUSG00000020611.15.
DR   GeneID; 14674; -.
DR   KEGG; mmu:14674; -.
DR   UCSC; uc007mce.1; mouse.
DR   AGR; MGI:95768; -.
DR   CTD; 10672; -.
DR   MGI; MGI:95768; Gna13.
DR   VEuPathDB; HostDB:ENSMUSG00000020611; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   GeneTree; ENSGT00940000157054; -.
DR   HOGENOM; CLU_014184_3_1_1; -.
DR   InParanoid; P27601; -.
DR   OMA; RFACMRC; -.
DR   OrthoDB; 2897309at2759; -.
DR   PhylomeDB; P27601; -.
DR   TreeFam; TF300673; -.
DR   Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   BioGRID-ORCS; 14674; 11 hits in 83 CRISPR screens.
DR   ChiTaRS; Gna13; mouse.
DR   EvolutionaryTrace; P27601; -.
DR   PRO; PR:P27601; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P27601; Protein.
DR   Bgee; ENSMUSG00000020611; Expressed in rostral migratory stream and 261 other cell types or tissues.
DR   ExpressionAtlas; P27601; baseline and differential.
DR   GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; ISA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031752; F:D5 dopamine receptor binding; ISO:MGI.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISA:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR   GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0030168; P:platelet activation; IMP:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   GO; GO:0010762; P:regulation of fibroblast migration; IMP:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000469; Gprotein_alpha_12/13.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10218:SF85; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT ALPHA-13; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00440; GPROTEINA12.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
DR   Genevisible; P27601; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Nucleus; Palmitate; Phosphoprotein; Reference proteome; Transducer.
FT   CHAIN           1..377
FT                   /note="Guanine nucleotide-binding protein subunit alpha-13"
FT                   /id="PRO_0000203774"
FT   DOMAIN          47..377
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          50..63
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          195..203
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          218..227
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          287..294
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          347..352
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         58..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:16388592,
FT                   ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT                   ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:18940608,
FT                   ECO:0007744|PDB:3CX6"
FT   BINDING         173
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:18940608,
FT                   ECO:0007744|PDB:3CX7"
FT   BINDING         197..200
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:16388592,
FT                   ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT                   ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:18940608,
FT                   ECO:0007744|PDB:3CX6"
FT   BINDING         291..294
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:16388592,
FT                   ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT                   ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT   BINDING         349
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:16388592,
FT                   ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT                   ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT   MOD_RES         203
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14344"
FT   LIPID           14
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14344"
FT   LIPID           18
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14344"
FT   CONFLICT        52
FT                   /note="L -> P (in Ref. 2; AAH57665)"
FT                   /evidence="ECO:0000305"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           61..72
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           78..82
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           85..105
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           116..123
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           130..133
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           139..154
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           156..163
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           164..167
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           174..178
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           181..184
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   STRAND          185..188
FT                   /evidence="ECO:0007829|PDB:1SHZ"
FT   HELIX           193..198
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   STRAND          204..213
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   STRAND          216..223
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           227..236
FT                   /evidence="ECO:0007829|PDB:3CX8"
FT   STRAND          242..248
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:3AB3"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           264..276
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           279..281
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   STRAND          284..291
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           293..299
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   TURN            300..302
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           305..307
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           319..331
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   STRAND          343..346
FT                   /evidence="ECO:0007829|PDB:1ZCB"
FT   HELIX           352..371
FT                   /evidence="ECO:0007829|PDB:1ZCB"
SQ   SEQUENCE   377 AA;  44055 MW;  45A6A6DB47C707BB CRC64;
     MADFLPSRSV LSVCFPGCVL TNGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG
     KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNKNQLHGD
     KLMAFDTRAP MAAQGMVETR VFLQYLPAIR ALWEDSGIQN AYDRRREFQL GESVKYFLDN
     LDKLGVPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV
     TSILFLVSSS EFDQVLMEDR QTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV
     QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI NTENIRLVFR
     DVKDTILHDN LKQLMLQ
//