RB27A_MOUSE
ID RB27A_MOUSE Reviewed; 221 AA.
AC Q9ERI2;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ras-related protein Rab-27A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P51159};
GN Name=Rab27a;
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 STRAIN=C3H/HeSn;
RX PubMed=10859366; DOI=10.1073/pnas.140212797;
RA Wilson S.M., Yip R., Swing D.A., O'Sullivan T.N., Zhang Y., Novak E.K.,
RA Swank R.T., Russell L.B., Copeland N.G., Jenkins N.A.;
RT "A mutation in Rab27a causes the vesicle transport defects observed in
RT ashen mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7933-7938(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Izumi T.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP INTERACTION WITH SYTL5.
RX PubMed=12051743; DOI=10.1016/s0006-291x(02)00320-0;
RA Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT "Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal
RT tandem C2 domains.";
RL Biochem. Biophys. Res. Commun. 293:899-906(2002).
RN [6]
RP INTERACTION WITH SYTL1; SYTL2; SYTL3; SYTL4; SLAC2B AND MYRIP.
RX PubMed=11773082; DOI=10.1074/jbc.m112414200;
RA Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT functions as a novel Rab27A binding domain.";
RL J. Biol. Chem. 277:9212-9218(2002).
RN [7]
RP INTERACTION WITH MLPH.
RX PubMed=11887186; DOI=10.1038/ncb760;
RA Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E.,
RA Copeland N.G., Jenkins N.A., Hammer J.A. III;
RT "Identification of an organelle receptor for myosin-Va.";
RL Nat. Cell Biol. 4:271-278(2002).
RN [8]
RP INTERACTION WITH RPH3A AND RPH3AL.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [9]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SYTL2.
RX PubMed=16716193; DOI=10.1111/j.1365-2443.2006.00964.x;
RA Saegusa C., Tanaka T., Tani S., Itohara S., Mikoshiba K., Fukuda M.;
RT "Decreased basal mucus secretion by Slp2-a-deficient gastric surface mucous
RT cells.";
RL Genes Cells 11:623-631(2006).
RN [10]
RP INTERACTION WITH UNC13D.
RX PubMed=18354201; DOI=10.4049/jimmunol.180.7.4774;
RA Higashio H., Nishimura N., Ishizaki H., Miyoshi J., Orita S., Sakane A.,
RA Sasaki T.;
RT "Doc2 alpha and Munc13-4 regulate Ca(2+) -dependent secretory lysosome
RT exocytosis in mast cells.";
RL J. Immunol. 180:4774-4784(2008).
RN [11]
RP INTERACTION WITH SYTL1 AND SYTL2.
RX PubMed=18266782; DOI=10.1111/j.1600-0854.2008.00714.x;
RA Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A., Arico M.,
RA Saegusa C., Fukuda M., Griffiths G.M.;
RT "Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute to
RT secretion from the immunological synapse.";
RL Traffic 9:446-457(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-193 IN COMPLEX WITH GTP ANALOG,
RP INTERACTION WITH SYTL2, AND MUTAGENESIS OF GLN-78.
RX PubMed=18940603; DOI=10.1016/j.str.2008.07.015;
RA Chavas L.M., Ihara K., Kawasaki M., Torii S., Uejima T., Kato R., Izumi T.,
RA Wakatsuki S.;
RT "Elucidation of Rab27 recruitment by its effectors: structure of Rab27a
RT bound to Exophilin4/Slp2-a.";
RL Structure 16:1468-1477(2008).
CC -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC inactive GDP-bound states. In its active state, binds to a variety of
CC effector proteins to regulate homeostasis of late endocytic pathway,
CC including endosomal positioning, maturation and secretion. Plays a role
CC in cytotoxic granule exocytosis in lymphocytes. Required for both
CC granule maturation and granule docking and priming at the immunologic
CC synapse. {ECO:0000250|UniProtKB:P51159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P51159};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P51159};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. Activated by GEFs such as DENND10.
CC {ECO:0000250|UniProtKB:P51159}.
CC -!- SUBUNIT: Binds SYTL1, SYTL2, SLAC2B, MYRIP, SYTL3, SYTL4, SYTL5 and
CC MLPH. Interacts with UNC13D. Interacts with RPH3A and RPH3A. Does not
CC interact with the BLOC-3 complex (heterodimer of HPS1 and HPS4) (By
CC similarity). Interacts (GDP-bound form preferentially) with DENND10 (By
CC similarity). {ECO:0000250|UniProtKB:P51159,
CC ECO:0000269|PubMed:11773082, ECO:0000269|PubMed:11887186,
CC ECO:0000269|PubMed:12051743, ECO:0000269|PubMed:12578829,
CC ECO:0000269|PubMed:16716193, ECO:0000269|PubMed:18266782,
CC ECO:0000269|PubMed:18354201, ECO:0000269|PubMed:18940603}.
CC -!- INTERACTION:
CC Q9ERI2; Q91V27: Mlph; NbExp=2; IntAct=EBI-398172, EBI-398308;
CC Q9ERI2; P47708: Rph3a; NbExp=2; IntAct=EBI-398172, EBI-398376;
CC Q9ERI2; Q9R0Q1-1: Sytl4; NbExp=2; IntAct=EBI-398172, EBI-15734647;
CC Q9ERI2; Q9HCH5: SYTL2; Xeno; NbExp=4; IntAct=EBI-398172, EBI-2690103;
CC Q9ERI2; Q8TDW5: SYTL5; Xeno; NbExp=2; IntAct=EBI-398172, EBI-2939487;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P51159}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P51159}. Melanosome
CC {ECO:0000250|UniProtKB:P51159}. Late endosome
CC {ECO:0000250|UniProtKB:P51159}. Lysosome
CC {ECO:0000250|UniProtKB:P51159}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV. Localizes to endosomal
CC exocytic vesicles. {ECO:0000250|UniProtKB:P51159}.
CC -!- TISSUE SPECIFICITY: Detected in melanocytes. Expressed abundantly in
CC the stomach and is predominantly localized at the apical region of
CC gastric-surface mucus cells. Also expressed in the thymus and lung.
CC {ECO:0000269|PubMed:16716193}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF304376; AAG24638.1; -; mRNA.
DR EMBL; AB046693; BAB62313.1; -; mRNA.
DR EMBL; AK010373; BAB26891.1; -; mRNA.
DR EMBL; BC008173; AAH08173.1; -; mRNA.
DR EMBL; BC009656; AAH09656.1; -; mRNA.
DR CCDS; CCDS23335.1; -.
DR RefSeq; NP_001288159.1; NM_001301230.1.
DR RefSeq; NP_001288161.1; NM_001301232.1.
DR RefSeq; NP_076124.1; NM_023635.6.
DR RefSeq; XP_006510843.1; XM_006510780.3.
DR PDB; 3BC1; X-ray; 1.80 A; A/E=1-193.
DR PDBsum; 3BC1; -.
DR AlphaFoldDB; Q9ERI2; -.
DR SMR; Q9ERI2; -.
DR BioGRID; 198222; 7.
DR CORUM; Q9ERI2; -.
DR DIP; DIP-31054N; -.
DR IntAct; Q9ERI2; 13.
DR STRING; 10090.ENSMUSP00000034722; -.
DR iPTMnet; Q9ERI2; -.
DR PhosphoSitePlus; Q9ERI2; -.
DR EPD; Q9ERI2; -.
DR jPOST; Q9ERI2; -.
DR MaxQB; Q9ERI2; -.
DR PaxDb; Q9ERI2; -.
DR PRIDE; Q9ERI2; -.
DR ProteomicsDB; 300247; -.
DR Antibodypedia; 687; 470 antibodies from 38 providers.
DR DNASU; 11891; -.
DR Ensembl; ENSMUST00000034722; ENSMUSP00000034722; ENSMUSG00000032202.
DR Ensembl; ENSMUST00000184146; ENSMUSP00000139310; ENSMUSG00000032202.
DR GeneID; 11891; -.
DR KEGG; mmu:11891; -.
DR UCSC; uc009qqv.2; mouse.
DR CTD; 5873; -.
DR MGI; MGI:1861441; Rab27a.
DR VEuPathDB; HostDB:ENSMUSG00000032202; -.
DR eggNOG; KOG0081; Eukaryota.
DR GeneTree; ENSGT00940000156218; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q9ERI2; -.
DR OMA; CTGANIQ; -.
DR OrthoDB; 1190514at2759; -.
DR PhylomeDB; Q9ERI2; -.
DR TreeFam; TF312895; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 11891; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Rab27a; mouse.
DR EvolutionaryTrace; Q9ERI2; -.
DR PRO; PR:Q9ERI2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ERI2; protein.
DR Bgee; ENSMUSG00000032202; Expressed in granulocyte and 208 other tissues.
DR ExpressionAtlas; Q9ERI2; baseline and differential.
DR Genevisible; Q9ERI2; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0070382; C:exocytic vesicle; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IMP:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR GO; GO:0033093; C:Weibel-Palade body; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; IPI:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0097278; P:complement-dependent cytotoxicity; ISO:MGI.
DR GO; GO:0043316; P:cytotoxic T cell degranulation; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; ISO:MGI.
DR GO; GO:1990182; P:exosomal secretion; ISO:MGI.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
DR GO; GO:0032400; P:melanosome localization; ISO:MGI.
DR GO; GO:0032402; P:melanosome transport; IMP:MGI.
DR GO; GO:0036257; P:multivesicular body organization; ISO:MGI.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0043320; P:natural killer cell degranulation; IMP:MGI.
DR GO; GO:0051875; P:pigment granule localization; IMP:MGI.
DR GO; GO:0051904; P:pigment granule transport; IMP:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:1903435; P:positive regulation of constitutive secretory pathway; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:1903307; P:positive regulation of regulated secretory pathway; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:MGI.
DR CDD; cd04127; Rab27A; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041837; Rab27a/b.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disulfide bond; Endosome; Exocytosis;
KW GTP-binding; Hydrolase; Lipoprotein; Lysosome; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51159"
FT CHAIN 2..221
FT /note="Ras-related protein Rab-27A"
FT /id="PRO_0000121222"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 163..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P51159"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51159"
FT MOD_RES 221
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 219
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 221
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 123..188
FT /evidence="ECO:0000250"
FT MUTAGEN 78
FT /note="Q->L: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:18940603"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3BC1"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:3BC1"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:3BC1"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:3BC1"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:3BC1"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3BC1"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:3BC1"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3BC1"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 170..187
FT /evidence="ECO:0007829|PDB:3BC1"
SQ SEQUENCE 221 AA; 25017 MW; C6857EBDD7F38137 CRC64;
MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR VVYRANGPDG
AVGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD LTNEQSFLNV RNWISQLQMH
AYCENPDIVL CGNKSDLEDQ RAVKEEEARE LAEKYGIPYF ETSAANGTNI SHAIEMLLDL
IMKRMERCVD KSWIPEGVVR SNGHTSADQL SEEKEKGLCG C
