ID   PACRG_HUMAN             Reviewed;         296 AA.
AC   Q96M98; E1P5B5; Q6IMB8; Q8IZM1; Q8NHP5; Q9H1V9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Parkin coregulated gene protein;
DE   AltName: Full=Molecular chaperone/chaperonin-binding protein;
DE   AltName: Full=PARK2 coregulated gene protein;
GN   Name=PACRG; Synonyms=GLUP;
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 2).
RX   PubMed=12547187; DOI=10.1016/s0022-2836(02)01376-1;
RA   West A.B., Lockhart P.J., O'Farell C., Farrer M.J.;
RT   "Identification of a novel gene linked to parkin via a bi-directional
RT   promoter.";
RL   J. Mol. Biol. 326:11-19(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [6]
RP   IDENTIFICATION, FUNCTION, AND INTERACTION WITH STIP1; PRKN; GPR37; HSPA8;
RP   TCP1; CCT2; CCT3; CCT4; CCT5; CCT6A; CCT7 AND CCT8.
RX   PubMed=14532270; DOI=10.1074/jbc.m309655200;
RA   Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT   "A product of the human gene adjacent to parkin is a component of Lewy
RT   bodies and suppresses Pael receptor-induced cell death.";
RL   J. Biol. Chem. 278:51901-51910(2003).
RN   [7] {ECO:0007744|PDB:7UNG}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=36191189; DOI=10.1073/pnas.2207605119;
RA   Gui M., Croft J.T., Zabeo D., Acharya V., Kollman J.M., Burgoyne T.,
RA   Hoog J.L., Brown A.;
RT   "SPACA9 is a lumenal protein of human ciliary singlet and doublet
RT   microtubules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:e2207605119-e2207605119(2022).
RN   [8]
RP   TISSUE SPECIFICITY, POLYMORPHISM, AND INVOLVEMENT IN LPRS2.
RX   PubMed=14737177; DOI=10.1038/nature02326;
RA   Mira M.T., Alcais A., Nguyen V.T., Moraes M.O., Di Flumeri C., Vu H.T.,
RA   Mai C.P., Nguyen T.H., Nguyen N.B., Pham X.K., Sarno E.N., Alter A.,
RA   Montpetit A., Moraes M.E., Moraes J.R., Dore C., Gallant C.J., Lepage P.,
RA   Verner A., Van De Vosse E., Hudson T.J., Abel L., Schurr E.;
RT   "Susceptibility to leprosy is associated with PARK2 and PACRG.";
RL   Nature 427:636-640(2004).
CC   -!- FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated
CC       doublet microtubules (DMTs) in cilia axoneme, which is required for
CC       motile cilia beating (PubMed:36191189). Suppresses cell death induced
CC       by accumulation of unfolded Pael receptor (Pael-R, a substrate of
CC       Parkin). Facilitates the formation of inclusions consisting of Pael-R,
CC       molecular chaperones, protein degradation molecules and itself when
CC       proteasome is inhibited. May play an important role in the formation of
CC       Lewy bodies and protection of dopaminergic neurons against Parkinson
CC       disease (PubMed:14532270). {ECO:0000250|UniProtKB:A5PK71,
CC       ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:36191189}.
CC   -!- SUBUNIT: Forms a large molecular chaperone complex containing heat
CC       shock proteins 70 and 90 and chaperonin components. Interacts with
CC       STIP1, PRKN, GPR37, HSPA8, TCP1/CCT1, CCT2, CCT3, CCT4, CCT5, CCT6A,
CC       CCT7, CCT8. Interacts with MEIG1 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96M98-2; Q5JSS6: MEIG1; NbExp=5; IntAct=EBI-11945452, EBI-18583441;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:36191189}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96M98-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96M98-2; Sequence=VSP_010033;
CC   -!- TISSUE SPECIFICITY: Expressed in all immune tissues, spleen, lymph
CC       nodes, thymus, tonsils, leukocyte and bone marrow. Expressed also in
CC       heart, brain, skeletal muscle, kidney, lung and pancreas. Expressed in
CC       primary Schwann cells and very weakly by monocyte-derived macrophages
CC       the primary host cells of Mycobacterium leprae, the causative agent of
CC       leprosy. Component of Lewy bodies, intraneuronal inclusions found in
CC       the brain of Parkinson disease patients. {ECO:0000269|PubMed:14737177,
CC       ECO:0000269|PubMed:36191189}.
CC   -!- POLYMORPHISM: Involved in susceptibility to leprosy (LPRS2)
CC       [MIM:607572]. LPRS2 is associated with polymorphisms in the 5'-
CC       regulatory region shared by the PRKN gene.
CC       {ECO:0000269|PubMed:14737177}.
CC   -!- MISCELLANEOUS: Linked to PRKN in a head-to-head arrangement on opposite
CC       DNA strands and share a common 5'-flanking promoter region.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
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DR   EMBL; AF546872; AAN37911.1; -; mRNA.
DR   EMBL; AK057286; BAB71410.1; -; mRNA.
DR   EMBL; AL031121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL078585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL603788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW47565.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW47566.1; -; Genomic_DNA.
DR   EMBL; BC030642; AAH30642.1; -; mRNA.
DR   EMBL; BC044227; AAH44227.1; -; mRNA.
DR   EMBL; BK001670; DAA02134.1; -; mRNA.
DR   CCDS; CCDS43524.1; -. [Q96M98-2]
DR   CCDS; CCDS5284.1; -. [Q96M98-1]
DR   RefSeq; NP_001073847.1; NM_001080378.1. [Q96M98-2]
DR   RefSeq; NP_001073848.1; NM_001080379.1. [Q96M98-2]
DR   RefSeq; NP_689623.2; NM_152410.2. [Q96M98-1]
DR   PDB; 6NDU; X-ray; 2.10 A; A=70-296.
DR   PDB; 6NEP; X-ray; 2.10 A; A=70-296.
DR   PDB; 6UCC; X-ray; 2.60 A; A=1-296.
DR   PDB; 7UNG; EM; 3.60 A; YB/YC/YD/YE/YF/YG=1-296.
DR   PDB; 8J07; EM; 4.10 A; YB/YC/YD/YF/YG/YH/YI/YJ/YK/YL/YM=1-296.
DR   PDBsum; 6NDU; -.
DR   PDBsum; 6NEP; -.
DR   PDBsum; 6UCC; -.
DR   PDBsum; 7UNG; -.
DR   PDBsum; 8J07; -.
DR   AlphaFoldDB; Q96M98; -.
DR   EMDB; EMD-26624; -.
DR   EMDB; EMD-35888; -.
DR   SMR; Q96M98; -.
DR   BioGRID; 126421; 28.
DR   IntAct; Q96M98; 4.
DR   STRING; 9606.ENSP00000337946; -.
DR   iPTMnet; Q96M98; -.
DR   PhosphoSitePlus; Q96M98; -.
DR   BioMuta; PACRG; -.
DR   DMDM; 77416872; -.
DR   MassIVE; Q96M98; -.
DR   PaxDb; 9606-ENSP00000337946; -.
DR   PeptideAtlas; Q96M98; -.
DR   ProteomicsDB; 77323; -. [Q96M98-1]
DR   ProteomicsDB; 77324; -. [Q96M98-2]
DR   Antibodypedia; 20047; 181 antibodies from 26 providers.
DR   DNASU; 135138; -.
DR   Ensembl; ENST00000337019.7; ENSP00000337946.3; ENSG00000112530.13. [Q96M98-1]
DR   Ensembl; ENST00000366888.7; ENSP00000355854.2; ENSG00000112530.13. [Q96M98-2]
DR   Ensembl; ENST00000366889.6; ENSP00000355855.2; ENSG00000112530.13. [Q96M98-2]
DR   GeneID; 135138; -.
DR   KEGG; hsa:135138; -.
DR   MANE-Select; ENST00000366888.7; ENSP00000355854.2; NM_001080379.2; NP_001073848.1. [Q96M98-2]
DR   UCSC; uc003qua.4; human. [Q96M98-1]
DR   AGR; HGNC:19152; -.
DR   DisGeNET; 135138; -.
DR   GeneCards; PACRG; -.
DR   HGNC; HGNC:19152; PACRG.
DR   HPA; ENSG00000112530; Tissue enhanced (fallopian tube, testis).
DR   MalaCards; PACRG; -.
DR   MIM; 607572; phenotype.
DR   MIM; 608427; gene.
DR   neXtProt; NX_Q96M98; -.
DR   OpenTargets; ENSG00000112530; -.
DR   PharmGKB; PA134909011; -.
DR   VEuPathDB; HostDB:ENSG00000112530; -.
DR   eggNOG; KOG3961; Eukaryota.
DR   GeneTree; ENSGT00940000157330; -.
DR   HOGENOM; CLU_073223_1_0_1; -.
DR   InParanoid; Q96M98; -.
DR   OMA; INGPIHE; -.
DR   OrthoDB; 128163at2759; -.
DR   PhylomeDB; Q96M98; -.
DR   TreeFam; TF321123; -.
DR   PathwayCommons; Q96M98; -.
DR   SignaLink; Q96M98; -.
DR   SIGNOR; Q96M98; -.
DR   BioGRID-ORCS; 135138; 7 hits in 1141 CRISPR screens.
DR   ChiTaRS; PACRG; human.
DR   GeneWiki; PACRG; -.
DR   GenomeRNAi; 135138; -.
DR   Pharos; Q96M98; Tbio.
DR   PRO; PR:Q96M98; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q96M98; Protein.
DR   Bgee; ENSG00000112530; Expressed in bronchial epithelial cell and 124 other cell types or tissues.
DR   ExpressionAtlas; Q96M98; baseline and differential.
DR   GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR   GO; GO:0044297; C:cell body; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0002177; C:manchette; IEA:Ensembl.
DR   GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR   GO; GO:0031982; C:vesicle; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0003779; F:actin binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0043014; F:alpha-tubulin binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0048487; F:beta-tubulin binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0030544; F:Hsp70 protein binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0051879; F:Hsp90 protein binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0034620; P:cellular response to unfolded protein; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR   GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR   InterPro; IPR019399; Parkin_co-regulated_protein.
DR   PANTHER; PTHR21207:SF2; PARKIN COREGULATED GENE PROTEIN; 1.
DR   PANTHER; PTHR21207; PARKIN COREGULATED GENE PROTEIN PARK2 COREGULATED; 1.
DR   Pfam; PF10274; ParcG; 2.
DR   Genevisible; Q96M98; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW   Cytoskeleton; Reference proteome.
FT   CHAIN           1..296
FT                   /note="Parkin coregulated gene protein"
FT                   /id="PRO_0000058169"
FT   VAR_SEQ         205..243
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12547187,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010033"
FT   CONFLICT        93
FT                   /note="K -> R (in Ref. 2; BAB71410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="A -> T (in Ref. 5; AAH30642)"
FT                   /evidence="ECO:0000305"
FT   HELIX           70..77
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:6UCC"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           123..138
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           146..157
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           162..178
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           182..186
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           190..193
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           260..274
FT                   /evidence="ECO:0007829|PDB:6NEP"
FT   HELIX           279..286
FT                   /evidence="ECO:0007829|PDB:6NEP"
SQ   SEQUENCE   296 AA;  33342 MW;  4A415741D430C7FB CRC64;
     MVAEKETLSL NKCPDKMPKR TKLLAQQPLP VHQPHSLVSE GFTVKAMMKN SVVRGPPAAG
     AFKERPTKPT AFRKFYERGD FPIALEHDSK GNKIAWKVEI EKLDYHHYLP LFFDGLCEMT
     FPYEFFARQG IHDMLEHGGN KILPVLPQLI IPIKNALNLR NRQVICVTLK VLQHLVVSAE
     MVGKALVPYY RQILPVLNIF KNMNGSYSLP RLECSGAIMA RCNLDHLGSS DPPTSASQVA
     EIIVNSGDGI DYSQQKRENI GDLIQETLEA FERYGGENAF INIKYVVPTY ESCLLN
//