TSPO_MOUSE
ID TSPO_MOUSE Reviewed; 169 AA.
AC P50637; Q541E3; Q62118; Q6LCZ0; Q99M32;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Translocator protein;
DE AltName: Full=Mitochondrial benzodiazepine receptor;
DE AltName: Full=PKBS;
DE AltName: Full=Peripheral-type benzodiazepine receptor;
DE Short=PBR;
GN Name=Tspo; Synonyms=Bzrp, Mbr;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=8114671;
RA Garnier M., Dimchev A.B., Boujrad N., Price J.M., Musto N.A.,
RA Papadopoulos V.;
RT "In vitro reconstitution of a functional peripheral-type benzodiazepine
RT receptor from mouse Leydig tumor cells.";
RL Mol. Pharmacol. 45:201-211(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Erythroleukemia;
RX PubMed=8125973; DOI=10.1016/s0021-9258(17)37318-0;
RA Taketani S., Kohno H., Okuda M., Furukawa T., Tokunaga R.;
RT "Induction of peripheral-type benzodiazepine receptors during
RT differentiation of mouse erythroleukemia cells. A possible involvement of
RT these receptors in heme biosynthesis.";
RL J. Biol. Chem. 269:7527-7531(1994).
RN [3] {ECO:0000312|EMBL:AAL87530.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS {ECO:0000312|EMBL:AAL87529.1}, and
RC ISS {ECO:0000312|EMBL:AAL87530.1};
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE29056.1}, and
RC NOD {ECO:0000312|EMBL:BAE33730.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE29056.1},
RC Kidney {ECO:0000312|EMBL:BAE38192.1}, Lung {ECO:0000312|EMBL:BAE38585.1},
RC Spleen {ECO:0000312|EMBL:BAE33730.1}, and
RC Uterus {ECO:0000312|EMBL:BAE38396.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH02055.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH02055.1};
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-125.
RX PubMed=7721091; DOI=10.1016/0378-1119(94)00817-c;
RA Yakovlev A.G., Ruffo M., Jurka J., Krueger K.E.;
RT "Comparison of repetitive elements in the third intron of human and rodent
RT mitochondrial benzodiazepine receptor-encoding genes.";
RL Gene 155:201-205(1995).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF TYR-153 AND ARG-156.
RX PubMed=9832438; DOI=10.1210/endo.139.12.6390;
RA Li H., Papadopoulos V.;
RT "Peripheral-type benzodiazepine receptor function in cholesterol transport.
RT Identification of a putative cholesterol recognition/interaction amino acid
RT sequence and consensus pattern.";
RL Endocrinology 139:4991-4997(1998).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Spleen;
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 [10]
RP FUNCTION.
RX PubMed=24814875; DOI=10.1042/cs20140047;
RA Taylor J.M., Allen A.M., Graham A.;
RT "Targeting mitochondrial 18kDa translocator protein (TSPO) regulates
RT macrophage cholesterol efflux and lipid phenotype.";
RL Clin. Sci. 127:603-613(2014).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24174323; DOI=10.1210/en.2013-1556;
RA Morohaku K., Pelton S.H., Daugherty D.J., Butler W.R., Deng W.,
RA Selvaraj V.;
RT "Translocator protein/peripheral benzodiazepine receptor is not required
RT for steroid hormone biosynthesis.";
RL Endocrinology 155:89-97(2014).
RN [12]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24936060; DOI=10.1074/jbc.m114.578286;
RA Tu L.N., Morohaku K., Manna P.R., Pelton S.H., Butler W.R., Stocco D.M.,
RA Selvaraj V.;
RT "Peripheral benzodiazepine receptor/translocator protein global knockout
RT mice are viable with no effects on steroid hormone biosynthesis.";
RL J. Biol. Chem. 289:27444-27454(2014).
RN [13]
RP STRUCTURE BY NMR IN COMPLEX WITH SYNTHETIC LIGAND PK11195, TOPOLOGY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24653034; DOI=10.1126/science.1248725;
RA Jaremko L., Jaremko M., Giller K., Becker S., Zweckstetter M.;
RT "Structure of the mitochondrial translocator protein in complex with a
RT diagnostic ligand.";
RL Science 343:1363-1366(2014).
RN [14] {ECO:0007744|PDB:2N02}
RP STRUCTURE BY NMR OF MUTANT THR-147 IN COMPLEX WITH SYNTHETIC LIGAND
RP PK11195, AND MUTAGENESIS OF ALA-147.
RX PubMed=25974690; DOI=10.1002/cbic.201500217;
RA Jaremko M., Jaremko L., Giller K., Becker S., Zweckstetter M.;
RT "Structural Integrity of the A147T Polymorph of Mammalian TSPO.";
RL ChemBioChem 16:1483-1489(2015).
CC -!- FUNCTION: Can bind protoporphyrin IX and may play a role in the
CC transport of porphyrins and heme (By similarity). Was initially
CC identified as peripheral-type benzodiazepine receptor; can also bind
CC isoquinoline carboxamides. Promotes the transport of cholesterol across
CC mitochondrial membranes and may play a role in lipid metabolism
CC (PubMed:9832438, PubMed:24814875), but its precise physiological role
CC is controversial. According to some reports, it is not required for
CC steroid hormone biosynthesis (PubMed:24174323, PubMed:24936060).
CC {ECO:0000250, ECO:0000269|PubMed:24174323, ECO:0000269|PubMed:24814875,
CC ECO:0000269|PubMed:24936060, ECO:0000269|PubMed:8114671,
CC ECO:0000269|PubMed:9832438}.
CC -!- SUBUNIT: Interacts with TSPOAP1. Interacts with MOST-1. May interact
CC with STAR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Ubiquitous.
CC {ECO:0000269|PubMed:24174323, ECO:0000269|PubMed:24936060}.
CC -!- INDUCTION: By dimethyl sulfoxide and diazepam.
CC {ECO:0000269|PubMed:8125973}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype. Mice are viable and fertile
CC and present only very minor changes in gonadal and adrenal steroid
CC hormone production. testis-specific gene disruption (PubMed:24174323)
CC does not affect testosterone production, gametogenesis and male
CC fertility. {ECO:0000269|PubMed:24174323, ECO:0000269|PubMed:24936060}.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; L17306; AAA20127.1; -; mRNA.
DR EMBL; D21207; BAA04749.1; -; mRNA.
DR EMBL; AY079441; AAL87529.1; -; Genomic_DNA.
DR EMBL; AY079442; AAL87530.1; -; Genomic_DNA.
DR EMBL; AK149743; BAE29056.1; -; mRNA.
DR EMBL; AK150516; BAE29628.1; -; mRNA.
DR EMBL; AK151421; BAE30386.1; -; mRNA.
DR EMBL; AK151569; BAE30511.1; -; mRNA.
DR EMBL; AK151824; BAE30721.1; -; mRNA.
DR EMBL; AK152082; BAE30932.1; -; mRNA.
DR EMBL; AK152827; BAE31528.1; -; mRNA.
DR EMBL; AK153159; BAE31769.1; -; mRNA.
DR EMBL; AK153273; BAE31860.1; -; mRNA.
DR EMBL; AK156489; BAE33730.1; -; mRNA.
DR EMBL; AK165450; BAE38192.1; -; mRNA.
DR EMBL; AK165822; BAE38396.1; -; mRNA.
DR EMBL; AK166125; BAE38585.1; -; mRNA.
DR EMBL; AK172384; BAE42976.1; -; mRNA.
DR EMBL; CH466550; EDL04468.1; -; Genomic_DNA.
DR EMBL; BC002055; AAH02055.1; -; mRNA.
DR EMBL; U12419; AAA83253.1; -; Genomic_DNA.
DR CCDS; CCDS27705.1; -.
DR PIR; A53405; A53405.
DR PIR; I57953; I57953.
DR RefSeq; NP_033905.3; NM_009775.4.
DR PDB; 2MGY; NMR; -; A=1-167.
DR PDB; 2N02; NMR; -; A=1-169.
DR PDBsum; 2MGY; -.
DR PDBsum; 2N02; -.
DR AlphaFoldDB; P50637; -.
DR BMRB; P50637; -.
DR SMR; P50637; -.
DR BioGRID; 198410; 2.
DR STRING; 10090.ENSMUSP00000037039; -.
DR BindingDB; P50637; -.
DR ChEMBL; CHEMBL2149; -.
DR iPTMnet; P50637; -.
DR PhosphoSitePlus; P50637; -.
DR jPOST; P50637; -.
DR PaxDb; P50637; -.
DR PeptideAtlas; P50637; -.
DR PRIDE; P50637; -.
DR ProteomicsDB; 297667; -.
DR TopDownProteomics; P50637; -.
DR Antibodypedia; 27480; 290 antibodies from 40 providers.
DR DNASU; 12257; -.
DR Ensembl; ENSMUST00000047419; ENSMUSP00000037039; ENSMUSG00000041736.
DR GeneID; 12257; -.
DR KEGG; mmu:12257; -.
DR UCSC; uc007xbg.2; mouse.
DR CTD; 706; -.
DR MGI; MGI:88222; Tspo.
DR VEuPathDB; HostDB:ENSMUSG00000041736; -.
DR eggNOG; KOG3797; Eukaryota.
DR GeneTree; ENSGT00390000012980; -.
DR HOGENOM; CLU_091805_2_1_1; -.
DR InParanoid; P50637; -.
DR OMA; GLNLIWM; -.
DR OrthoDB; 1592225at2759; -.
DR PhylomeDB; P50637; -.
DR TreeFam; TF342852; -.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR BioGRID-ORCS; 12257; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Tspo; mouse.
DR PRO; PR:P50637; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P50637; protein.
DR Bgee; ENSMUSG00000041736; Expressed in thoracic mammary gland and 223 other tissues.
DR ExpressionAtlas; P50637; baseline and differential.
DR Genevisible; P50637; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005497; F:androgen binding; ISO:MGI.
DR GO; GO:0008503; F:benzodiazepine receptor activity; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0048266; P:behavioral response to pain; ISO:MGI.
DR GO; GO:0071476; P:cellular hypotonic response; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071294; P:cellular response to zinc ion; IEA:Ensembl.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0060242; P:contact inhibition; ISO:MGI.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0008347; P:glial cell migration; ISO:MGI.
DR GO; GO:0006811; P:ion transport; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0072656; P:maintenance of protein location in mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903579; P:negative regulation of ATP metabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903147; P:negative regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000853; P:negative regulation of corticosterone secretion; ISO:MGI.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0010823; P:negative regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; ISO:MGI.
DR GO; GO:1905144; P:response to acetylcholine; ISO:MGI.
DR GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0010266; P:response to vitamin B1; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006694; P:steroid biosynthetic process; ISO:MGI.
DR CDD; cd15904; TSPO_MBR; 1.
DR Gene3D; 1.20.1260.100; -; 1.
DR InterPro; IPR030164; TSPO.
DR InterPro; IPR038330; TspO/MBR-related_sf.
DR InterPro; IPR004307; TspO_MBR.
DR PANTHER; PTHR10057; PTHR10057; 1.
DR PANTHER; PTHR10057:SF5; PTHR10057:SF5; 1.
DR Pfam; PF03073; TspO_MBR; 1.
DR PIRSF; PIRSF005859; PBR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid transport; Membrane; Mitochondrion; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..169
FT /note="Translocator protein"
FT /id="PRO_0000190998"
FT TOPO_DOM 1..5
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:24653034"
FT TRANSMEM 6..26
FT /note="Helical; Name=1"
FT TOPO_DOM 27..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24653034"
FT TRANSMEM 47..67
FT /note="Helical; Name=2"
FT TOPO_DOM 68..79
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:24653034"
FT TRANSMEM 80..100
FT /note="Helical; Name=3"
FT TOPO_DOM 101..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24653034"
FT TRANSMEM 106..126
FT /note="Helical; Name=4"
FT TOPO_DOM 127..134
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:24653034"
FT TRANSMEM 135..155
FT /note="Helical; Name=5"
FT TOPO_DOM 156..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24653034"
FT MUTAGEN 147
FT /note="A->T: No effect."
FT /evidence="ECO:0000269|PubMed:25974690"
FT MUTAGEN 153
FT /note="Y->S: Abolishes cholesterol transport."
FT /evidence="ECO:0000269|PubMed:9832438"
FT MUTAGEN 156
FT /note="R->L: Abolishes cholesterol transport."
FT /evidence="ECO:0000269|PubMed:9832438"
FT CONFLICT 36
FT /note="S -> G (in Ref. 6; AAH02055)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="G -> A (in Ref. 2; BAA04749)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="P -> A (in Ref. 2; BAA04749 and 6; AAH02055)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:2N02"
FT HELIX 6..36
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 52..71
FT /evidence="ECO:0007829|PDB:2MGY"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2MGY"
FT TURN 99..103
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:2MGY"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:2MGY"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2N02"
SQ SEQUENCE 169 AA; 18841 MW; 2EF93420C3842A85 CRC64;
MPESWVPAVG LTLVPSLGGF MGAYFVRGEG LRWYASLQKP SWHPPRWTLA PIWGTLYSAM
GYGSYIVWKE LGGFTEDAMV PLGLYTGQLA LNWAWPPIFF GARQMGWALA DLLLVSGVAT
ATTLAWHRVS PPAARLLYPY LAWLAFATVL NYYVWRDNSG RRGGSRLPE
