GA45A_HUMAN
ID GA45A_HUMAN Reviewed; 165 AA.
AC P24522; Q5TCA7; Q5TCA8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Growth arrest and DNA damage-inducible protein GADD45 alpha;
DE AltName: Full=DNA damage-inducible transcript 1 protein;
DE Short=DDIT-1;
GN Name=GADD45A; Synonyms=DDIT1, GADD45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1990262; DOI=10.1128/mcb.11.2.1009-1016.1991;
RA Papathanasiou M.A., Kerr N.C.K., Robbins J.H., McBride O.W., Alamo I. Jr.,
RA Barrett S.F., Hickson I.D., Fornace A.J. Jr.;
RT "Induction by ionizing radiation of the gadd45 gene in cultured human
RT cells: lack of mediation by protein kinase C.";
RL Mol. Cell. Biol. 11:1009-1016(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=8226988; DOI=10.1016/s0021-9258(20)80537-7;
RA Hollander M.C., Alamo I. Jr., Jackman J., Wang M.G., McBride O.W.,
RA Fornace A.J. Jr.;
RT "Analysis of the mammalian gadd45 gene and its response to DNA damage.";
RL J. Biol. Chem. 268:24385-24393(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Bronchiolar epithelial cell;
RX PubMed=16421274; DOI=10.1093/nar/gkj459;
RA Zhang Y., Bhatia D., Xia H., Castranova V., Shi X., Chen F.;
RT "Nucleolin links to arsenic-induced stabilization of GADD45alpha mRNA.";
RL Nucleic Acids Res. 34:485-495(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [9]
RP INTERACTION WITH GADD45GIP1.
RC TISSUE=Colon carcinoma;
RX PubMed=12716909; DOI=10.1074/jbc.m212835200;
RA Chung H.K., Yi Y.-W., Jung N.-C., Kim D., Suh J.M., Kim H., Park K.C.,
RA Song J.H., Kim D.W., Hwang E.S., Yoon S.-H., Bae Y.-S., Kim J.M., Bae I.,
RA Shong M.;
RT "CR6-interacting factor 1 interacts with Gadd45 family proteins and
RT modulates the cell cycle.";
RL J. Biol. Chem. 278:28079-28088(2003).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PCNA.
RX PubMed=7973727; DOI=10.1126/science.7973727;
RA Smith M.L., Chen I.-T., Zhan Q., Bae I., Chen C.-Y., Gilmer T.M.,
RA Kastan M.B., O'Connor P.M., Fornace A.J. Jr.;
RT "Interaction of the p53-regulated protein Gadd45 with proliferating cell
RT nuclear antigen.";
RL Science 266:1376-1380(1994).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP STRUCTURE BY NMR, SUBUNIT, INTERACTION WITH PCNA AND AURKA, AND MUTAGENESIS
RP OF LEU-77.
RX PubMed=20460379; DOI=10.1074/jbc.m109.069344;
RA Sanchez R., Pantoja-Uceda D., Prieto J., Diercks T., Marcaida M.J.,
RA Montoya G., Campos-Olivas R., Blanco F.J.;
RT "Solution structure of human growth arrest and DNA damage 45alpha
RT (Gadd45alpha) and its interactions with proliferating cell nuclear antigen
RT (PCNA) and Aurora A kinase.";
RL J. Biol. Chem. 285:22196-22201(2010).
CC -!- FUNCTION: In T-cells, functions as a regulator of p38 MAPKs by
CC inhibiting p88 phosphorylation and activity (By similarity). Might
CC affect PCNA interaction with some CDK (cell division protein kinase)
CC complexes; stimulates DNA excision repair in vitro and inhibits entry
CC of cells into S phase. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAPK14 (By similarity). Predominantly monomeric
CC but also forms dimers and other oligomers as concentration increases.
CC Interacts with GADD45GIP1. Interacts weakly with PCNA. Interacts with
CC AURKA, likely to compete with dimerization. {ECO:0000250,
CC ECO:0000269|PubMed:12716909, ECO:0000269|PubMed:20460379,
CC ECO:0000269|PubMed:7973727}.
CC -!- INTERACTION:
CC P24522; Q9GZX7: AICDA; NbExp=5; IntAct=EBI-448167, EBI-3834328;
CC P24522; Q92600-3: CNOT9; NbExp=5; IntAct=EBI-448167, EBI-12907584;
CC P24522; Q13561: DCTN2; NbExp=7; IntAct=EBI-448167, EBI-715074;
CC P24522; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-448167, EBI-356015;
CC P24522; P28715: ERCC5; NbExp=2; IntAct=EBI-448167, EBI-765885;
CC P24522; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-448167, EBI-372506;
CC P24522; Q92876: KLK6; NbExp=3; IntAct=EBI-448167, EBI-2432309;
CC P24522; P80303: NUCB2; NbExp=2; IntAct=EBI-448167, EBI-2296670;
CC P24522; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-448167, EBI-3921217;
CC P24522; Q9Y371: SH3GLB1; NbExp=2; IntAct=EBI-448167, EBI-2623095;
CC P24522; Q13569: TDG; NbExp=3; IntAct=EBI-448167, EBI-348333;
CC P24522; Q9WVE0: Aicda; Xeno; NbExp=3; IntAct=EBI-448167, EBI-3835567;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7973727}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P24522-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P24522-2; Sequence=VSP_042523;
CC -!- INDUCTION: By UV irradiation, X-rays, growth arrest and alkylating
CC agents. The induction is mediated by some kinase(s) other than PKC.
CC -!- SIMILARITY: Belongs to the GADD45 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gadd45a/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=GADD45A entry;
CC URL="https://en.wikipedia.org/wiki/GADD45A";
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DR EMBL; L24498; AAA72045.1; -; Genomic_DNA.
DR EMBL; M60974; AAA35863.1; -; mRNA.
DR EMBL; AY135686; AAM88884.1; -; Genomic_DNA.
DR EMBL; DQ008445; AAY25021.1; -; mRNA.
DR EMBL; AK314991; BAG37487.1; -; mRNA.
DR EMBL; AL136120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06487.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06488.1; -; Genomic_DNA.
DR EMBL; BC011757; AAH11757.1; -; mRNA.
DR CCDS; CCDS55605.1; -. [P24522-2]
DR CCDS; CCDS640.1; -. [P24522-1]
DR PIR; A39617; A39617.
DR RefSeq; NP_001186670.1; NM_001199741.1. [P24522-2]
DR RefSeq; NP_001186671.1; NM_001199742.1.
DR RefSeq; NP_001915.1; NM_001924.3. [P24522-1]
DR PDB; 2KG4; NMR; -; A=1-165.
DR PDBsum; 2KG4; -.
DR AlphaFoldDB; P24522; -.
DR BMRB; P24522; -.
DR SMR; P24522; -.
DR BioGRID; 108014; 102.
DR CORUM; P24522; -.
DR DIP; DIP-24217N; -.
DR IntAct; P24522; 65.
DR MINT; P24522; -.
DR STRING; 9606.ENSP00000360025; -.
DR iPTMnet; P24522; -.
DR PhosphoSitePlus; P24522; -.
DR BioMuta; GADD45A; -.
DR DMDM; 120751; -.
DR EPD; P24522; -.
DR MassIVE; P24522; -.
DR PaxDb; P24522; -.
DR PeptideAtlas; P24522; -.
DR PRIDE; P24522; -.
DR ProteomicsDB; 54209; -. [P24522-1]
DR Antibodypedia; 33411; 430 antibodies from 34 providers.
DR DNASU; 1647; -.
DR Ensembl; ENST00000370985.4; ENSP00000360024.3; ENSG00000116717.13. [P24522-2]
DR Ensembl; ENST00000370986.9; ENSP00000360025.4; ENSG00000116717.13. [P24522-1]
DR GeneID; 1647; -.
DR KEGG; hsa:1647; -.
DR MANE-Select; ENST00000370986.9; ENSP00000360025.4; NM_001924.4; NP_001915.1.
DR UCSC; uc001ddz.3; human. [P24522-1]
DR CTD; 1647; -.
DR DisGeNET; 1647; -.
DR GeneCards; GADD45A; -.
DR HGNC; HGNC:4095; GADD45A.
DR HPA; ENSG00000116717; Tissue enhanced (skeletal).
DR MIM; 126335; gene.
DR neXtProt; NX_P24522; -.
DR OpenTargets; ENSG00000116717; -.
DR PharmGKB; PA28510; -.
DR VEuPathDB; HostDB:ENSG00000116717; -.
DR eggNOG; ENOG502RY8P; Eukaryota.
DR GeneTree; ENSGT00950000182964; -.
DR HOGENOM; CLU_118164_0_0_1; -.
DR InParanoid; P24522; -.
DR OMA; CLLVDFP; -.
DR OrthoDB; 1517160at2759; -.
DR PhylomeDB; P24522; -.
DR TreeFam; TF300196; -.
DR PathwayCommons; P24522; -.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-9617828; FOXO-mediated transcription of cell cycle genes.
DR SignaLink; P24522; -.
DR SIGNOR; P24522; -.
DR BioGRID-ORCS; 1647; 15 hits in 1088 CRISPR screens.
DR ChiTaRS; GADD45A; human.
DR EvolutionaryTrace; P24522; -.
DR GeneWiki; GADD45A; -.
DR GenomeRNAi; 1647; -.
DR Pharos; P24522; Tbio.
DR PRO; PR:P24522; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P24522; protein.
DR Bgee; ENSG00000116717; Expressed in descending thoracic aorta and 200 other tissues.
DR ExpressionAtlas; P24522; baseline and differential.
DR Genevisible; P24522; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:CAFA.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:CAFA.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IMP:CACAO.
DR GO; GO:0033140; P:negative regulation of peptidyl-serine phosphorylation of STAT protein; IMP:CACAO.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:CACAO.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CACAO.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; IMP:BHF-UCL.
DR DisProt; DP00704; -.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR024824; GADD45.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR PANTHER; PTHR10411; PTHR10411; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; DNA damage; Growth arrest;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..165
FT /note="Growth arrest and DNA damage-inducible protein
FT GADD45 alpha"
FT /id="PRO_0000148331"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 15..49
FT /note="RMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNV -> S (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16421274"
FT /id="VSP_042523"
FT MUTAGEN 77
FT /note="L->E: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:20460379"
FT HELIX 16..33
FT /evidence="ECO:0007829|PDB:2KG4"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2KG4"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2KG4"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:2KG4"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2KG4"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2KG4"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2KG4"
FT HELIX 69..84
FT /evidence="ECO:0007829|PDB:2KG4"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2KG4"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:2KG4"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2KG4"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:2KG4"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:2KG4"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2KG4"
SQ SEQUENCE 165 AA; 18336 MW; F2ADC183F6C0F064 CRC64;
MTLEEFSAGE QKTERMDKVG DALEEVLSKA LSQRTITVGV YEAAKLLNVD PDNVVLCLLA
ADEDDDRDVA LQIHFTLIQA FCCENDINIL RVSNPGRLAE LLLLETDAGP AASEGAEQPP
DLHCVLVTNP HSSQWKDPAL SQLICFCRES RYMDQWVPVI NLPER
