RCCR_ARATH
ID RCCR_ARATH Reviewed; 319 AA.
AC Q8LDU4; O23185;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Red chlorophyll catabolite reductase, chloroplastic {ECO:0000303|PubMed:10743659};
DE Short=AtRCCR {ECO:0000303|PubMed:10743659};
DE Short=RCC reductase {ECO:0000305};
DE EC=1.3.7.12 {ECO:0000269|PubMed:10743659};
DE AltName: Full=Accelerated cell death protein 2 {ECO:0000303|PubMed:11149948};
DE Flags: Precursor;
GN Name=RCCR {ECO:0000303|PubMed:10743659};
GN Synonyms=ACD2 {ECO:0000303|PubMed:11149948};
GN OrderedLocusNames=At4g37000 {ECO:0000312|Araport:AT4G37000};
GN ORFNames=C7A10_360 {ECO:0000312|EMBL:CAB16763.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10743659; DOI=10.1046/j.1365-313x.2000.00667.x;
RA Wuethrich K.L., Bovet L., Hunziker P.E., Donnison I.S., Hoertensteiner S.;
RT "Molecular cloning, functional expression and characterization of RCC
RT reductase, involved in chlorophyll catabolism.";
RL Plant J. 21:189-198(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-140; 181-TYR--ASP-192 AND ARG-279.
RC STRAIN=cv. Columbia;
RX PubMed=11149948; DOI=10.1073/pnas.98.2.771;
RA Mach J.M., Castillo A.R., Hoogstraten R., Greenberg J.T.;
RT "The Arabidopsis accelerated cell death gene ACD2 encodes red chlorophyll
RT catabolite reductase and suppresses the spread of disease symptoms.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:771-776(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SGR1; NYC1; NOL; PAO; PPH AND
RP LHCII COMPLEX.
RX PubMed=22366162; DOI=10.1105/tpc.111.089474;
RA Sakuraba Y., Schelbert S., Park S.Y., Han S.H., Lee B.D., Andres C.B.,
RA Kessler F., Hortensteiner S., Paek N.C.;
RT "STAY-GREEN and chlorophyll catabolic enzymes interact at light-harvesting
RT complex II for chlorophyll detoxification during leaf senescence in
RT Arabidopsis.";
RL Plant Cell 24:507-518(2012).
RN [9]
RP INTERACTION WITH HCAR, AND DEVELOPMENTAL STAGE.
RX PubMed=23200839; DOI=10.1016/j.bbrc.2012.11.050;
RA Sakuraba Y., Kim Y.S., Yoo S.C., Hortensteiner S., Paek N.C.;
RT "7-Hydroxymethyl chlorophyll a reductase functions in metabolic channeling
RT of chlorophyll breakdown intermediates during leaf senescence.";
RL Biochem. Biophys. Res. Commun. 430:32-37(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 40-319, AND SUBUNIT.
RX PubMed=19374909; DOI=10.1016/j.jmb.2009.04.017;
RA Sugishima M., Kitamori Y., Noguchi M., Kohchi T., Fukuyama K.;
RT "Crystal structure of red chlorophyll catabolite reductase: enlargement of
RT the ferredoxin-dependent bilin reductase family.";
RL J. Mol. Biol. 389:376-387(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 49-319 IN COMPLEX WITH RED
RP CHLOROPHYLL CATABOLITE, SUBUNIT, AND MUTAGENESIS OF PHE-218.
RX PubMed=20727901; DOI=10.1016/j.jmb.2010.08.021;
RA Sugishima M., Okamoto Y., Noguchi M., Kohchi T., Tamiaki H., Fukuyama K.;
RT "Crystal structures of the substrate-bound forms of red chlorophyll
RT catabolite reductase: implications for site-specific and stereospecific
RT reaction.";
RL J. Mol. Biol. 402:879-891(2010).
CC -!- FUNCTION: Catalyzes the key reaction of chlorophyll catabolism,
CC porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary
CC fluorescent catabolite (pFCC). Works in a two-step reaction with
CC pheophorbide a oxygenase (PaO) by reducing the C20/C1 double bond of
CC the intermediate, RCC. Belongs to the chlorophyll catabolic enzymes
CC (CCEs). {ECO:0000269|PubMed:10743659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 oxidized [2Fe-2S]-[ferredoxin] + primary fluorescent
CC chlorophyll catabolite = 3 H(+) + red chlorophyll catabolite + 2
CC reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24752, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58716,
CC ChEBI:CHEBI:77670; EC=1.3.7.12;
CC Evidence={ECO:0000269|PubMed:10743659};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24754;
CC Evidence={ECO:0000269|PubMed:10743659};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC degradation. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (PubMed:19374909, PubMed:20727901). Interacts with
CC HCAR (PubMed:23200839). Interacts with SGR1, NYC1, NOL, PPH, PAO and
CC the LHCII complex (PubMed:22366162). Part of a SGR1-CCE-LHCII complex,
CC which acts in chlorophyll breakdown (PubMed:22366162).
CC {ECO:0000269|PubMed:19374909, ECO:0000269|PubMed:20727901,
CC ECO:0000269|PubMed:22366162, ECO:0000269|PubMed:23200839}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast
CC thylakoid membrane. Note=And a low amount in mitochondria of 7-day-old
CC seedlings.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including roots.
CC -!- DEVELOPMENTAL STAGE: Present at all times of development. No change of
CC levels during senescence or pathogen attack.
CC {ECO:0000269|PubMed:23200839}.
CC -!- MISCELLANEOUS: The absence of light completely suppresses cell death in
CC acd2 mutants.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF326347; AAG53980.1; -; mRNA.
DR EMBL; Z99707; CAB16763.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80366.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86733.1; -; Genomic_DNA.
DR EMBL; AY045578; AAK73936.1; -; mRNA.
DR EMBL; AY093785; AAM10401.1; -; mRNA.
DR EMBL; AY085797; AAM63013.1; -; mRNA.
DR PIR; A85437; A85437.
DR RefSeq; NP_195417.1; NM_119863.4.
DR PDB; 2ZXK; X-ray; 2.50 A; A/B=40-319.
DR PDB; 2ZXL; X-ray; 2.40 A; A/B=40-319.
DR PDB; 3AGA; X-ray; 2.60 A; A/B=49-319.
DR PDB; 3AGB; X-ray; 2.20 A; A/B=49-319.
DR PDB; 3AGC; X-ray; 2.00 A; A/B=49-319.
DR PDBsum; 2ZXK; -.
DR PDBsum; 2ZXL; -.
DR PDBsum; 3AGA; -.
DR PDBsum; 3AGB; -.
DR PDBsum; 3AGC; -.
DR AlphaFoldDB; Q8LDU4; -.
DR SMR; Q8LDU4; -.
DR BioGRID; 15135; 9.
DR IntAct; Q8LDU4; 2.
DR MINT; Q8LDU4; -.
DR STRING; 3702.AT4G37000.1; -.
DR PaxDb; Q8LDU4; -.
DR PRIDE; Q8LDU4; -.
DR ProteomicsDB; 225941; -.
DR EnsemblPlants; AT4G37000.1; AT4G37000.1; AT4G37000.
DR GeneID; 829854; -.
DR Gramene; AT4G37000.1; AT4G37000.1; AT4G37000.
DR KEGG; ath:AT4G37000; -.
DR Araport; AT4G37000; -.
DR TAIR; locus:2115105; AT4G37000.
DR eggNOG; ENOG502QSTY; Eukaryota.
DR HOGENOM; CLU_073200_0_0_1; -.
DR InParanoid; Q8LDU4; -.
DR OMA; WIRFPYL; -.
DR OrthoDB; 1382571at2759; -.
DR PhylomeDB; Q8LDU4; -.
DR BioCyc; ARA:AT4G37000-MON; -.
DR BioCyc; MetaCyc:AT4G37000-MON; -.
DR BRENDA; 1.3.7.12; 399.
DR UniPathway; UPA00674; -.
DR EvolutionaryTrace; Q8LDU4; -.
DR PRO; PR:Q8LDU4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LDU4; baseline and differential.
DR Genevisible; Q8LDU4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0051743; F:red chlorophyll catabolite reductase activity; IDA:TAIR.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:0010363; P:regulation of plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:TAIR.
DR InterPro; IPR009439; RCC_reductase.
DR PANTHER; PTHR34685; PTHR34685; 1.
DR Pfam; PF06405; RCC_reductase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll catabolism; Chloroplast; Coiled coil; Membrane;
KW NADP; Oxidoreductase; Plastid; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..319
FT /note="Red chlorophyll catabolite reductase, chloroplastic"
FT /id="PRO_0000022201"
FT COILED 255..286
FT /evidence="ECO:0000255"
FT BINDING 154
FT /ligand="red chlorophyll catabolite"
FT /ligand_id="ChEBI:CHEBI:58716"
FT /evidence="ECO:0000269|PubMed:20727901,
FT ECO:0007744|PDB:3AGA, ECO:0007744|PDB:3AGC"
FT BINDING 207..209
FT /ligand="red chlorophyll catabolite"
FT /ligand_id="ChEBI:CHEBI:58716"
FT /evidence="ECO:0000269|PubMed:20727901,
FT ECO:0007744|PDB:3AGA, ECO:0007744|PDB:3AGC"
FT BINDING 291
FT /ligand="red chlorophyll catabolite"
FT /ligand_id="ChEBI:CHEBI:58716"
FT /evidence="ECO:0000269|PubMed:20727901,
FT ECO:0007744|PDB:3AGA, ECO:0007744|PDB:3AGC"
FT SITE 218
FT /note="Important for stereospecificity of the product"
FT /evidence="ECO:0000269|PubMed:20727901"
FT MUTAGEN 140
FT /note="G->V: In acd2-12E13; spontaneous spreading cell
FT death lesions."
FT /evidence="ECO:0000269|PubMed:11149948"
FT MUTAGEN 181..192
FT /note="Missing: In acd2-7; spontaneous spreading cell death
FT lesions."
FT /evidence="ECO:0000269|PubMed:11149948"
FT MUTAGEN 218
FT /note="F->V: Induces switch of RCCR stereospecificity
FT product from pFCC-1 to pFCC-2."
FT /evidence="ECO:0000269|PubMed:20727901"
FT MUTAGEN 279
FT /note="R->K: In acd2-6; spontaneous spreading cell death
FT lesions."
FT /evidence="ECO:0000269|PubMed:11149948"
FT CONFLICT 290
FT /note="D -> E (in Ref. 7; AAM63013)"
FT /evidence="ECO:0000305"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2ZXL"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:2ZXL"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:3AGC"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 114..126
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2ZXL"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 151..168
FT /evidence="ECO:0007829|PDB:3AGC"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:3AGC"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 270..291
FT /evidence="ECO:0007829|PDB:3AGC"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:3AGC"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:3AGC"
SQ SEQUENCE 319 AA; 36449 MW; A46DC65FB7452517 CRC64;
MAMIFCNTLY SSSSPSYLSP LTSKPSRFSK NLRPRAQFQS MEDHDDHLRR KFMEFPYVSP
TRKQLMVDLM STVENRLQSQ LLPCNLPPDV RNFNNPNGSA EASLHIRSGD KSSPIDFVIG
SWIHCKIPTG VSLNITSISG FLNSSTKAPN FVVELIQSSS KSLVLILDLP HRKDLVLNPD
YLKEYYQDTA LDSHRQSLLK LPEVNPYVSP SLFVRSAFSP TASMLKIDAE EEDKLEEILR
DHVSPAAKEV LEVWLERCVK EEEEKIVVGE EERMELERRD KSFRRKSIED DLDLQFPRMF
GEEVSSRVVH AIKEAFGVL
