PRLD1_HUMAN
ID PRLD1_HUMAN Reviewed; 219 AA.
AC Q9Y255; B2R5F7; D6RD25; Q549N2; Q9UI13; Q9UJS9;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=PRELI domain-containing protein 1, mitochondrial;
DE AltName: Full=25 kDa protein of relevant evolutionary and lymphoid interest;
DE AltName: Full=Px19-like protein;
DE Flags: Precursor;
GN Name=PRELID1; Synonyms=PRELI; ORFNames=CGI-106, SBBI12;
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).
RC TISSUE=Tonsil;
RX PubMed=10784606; DOI=10.1093/intimm/12.5.607;
RA Guzman-Rojas L., Sims J.C., Rangel R., Guret C., Sun Y., Alcocer J.M.,
RA Martinez-Valdez H.;
RT "PRELI, the human homologue of the avian px19, is expressed by germinal
RT center B lymphocytes.";
RL Int. Immunol. 12:607-612(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang X.N., Yu L., Cui W.C., Zhang H.L., Xin Y.R., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to chicken px19 mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hair follicle dermal papilla;
RA Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y.,
RA Im S.U., Jung E.J., Lee J.H., Kim J.C.;
RT "A catalogue of genes in the human dermal papilla cells as identified by
RT expressed sequence tags.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Zhang W., He L., Wan T., Zhu X., Cao X.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Eye, Ovary, Placenta, and Uterus;
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 [11]
RP SUBCELLULAR LOCATION, AND PRESENCE OF N-TERMINAL TRANSIT PEPTIDE.
RX PubMed=14640972; DOI=10.1042/bj20031504;
RA Fox E.J., Stubbs S.A., Kyaw Tun J., Leek J.P., Markham A.F., Wright S.C.;
RT "PRELI (protein of relevant evolutionary and lymphoid interest) is located
RT within an evolutionarily conserved gene cluster on chromosome 5q34-q35 and
RT encodes a novel mitochondrial protein.";
RL Biochem. J. 378:817-825(2004).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18945965; DOI=10.1182/blood-2008-07-166553;
RA Tahvanainen J., Kallonen T., Lahteenmaki H., Heiskanen K.M.,
RA Westermarck J., Rao K.V., Lahesmaa R.;
RT "PRELI is a mitochondrial regulator of human primary T-helper cell
RT apoptosis, STAT6, and Th2-cell differentiation.";
RL Blood 113:1268-1277(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH OPA1 AND AIFM1.
RX PubMed=21364629; DOI=10.1038/cddis.2009.19;
RA McKeller M.R., Herrera-Rodriguez S., Ma W., Ortiz-Quintero B., Rangel R.,
RA Cande C., Sims-Mourtada J.C., Melnikova V., Kashi C., Phan L.M., Chen Z.,
RA Huang P., Dunner K. Jr., Kroemer G., Singh K.K., Martinez-Valdez H.;
RT "Vital function of PRELI and essential requirement of its LEA motif.";
RL Cell Death Dis. 1:E21-E21(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23931759; DOI=10.1016/j.cmet.2013.07.008;
RA Potting C., Tatsuta T., Konig T., Haag M., Wai T., Aaltonen M.J.,
RA Langer T.;
RT "TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial
RT transport of phosphatidic acid.";
RL Cell Metab. 18:287-295(2013).
CC -!- FUNCTION: Involved in the modulation of the mitochondrial apoptotic
CC pathway by ensuring the accumulation of cardiolipin (CL) in
CC mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates
CC the transfer of phosphatidic acid (PA) between liposomes and probably
CC functions as a PA transporter across the mitochondrion intermembrane
CC space to provide PA for CL synthesis in the inner membrane. Regulates
CC the mitochondrial apoptotic pathway in primary Th cells. Regulates Th
CC cell differentiation by down-regulating STAT6 thereby reducing IL-4-
CC induced Th2 cell number. May be important for the development of vital
CC and immunocompetent organs. {ECO:0000269|PubMed:18945965,
CC ECO:0000269|PubMed:21364629, ECO:0000269|PubMed:23931759}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-
CC glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608;
CC Evidence={ECO:0000269|PubMed:23931759};
CC -!- SUBUNIT: Forms a complex with TRIAP1 in the mitochondrion intermembrane
CC space. Interacts with OPA1 and AIFM1. {ECO:0000269|PubMed:21364629,
CC ECO:0000269|PubMed:23931759}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:14640972, ECO:0000269|PubMed:18945965,
CC ECO:0000269|PubMed:21364629, ECO:0000269|PubMed:23931759}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y255-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y255-2; Sequence=VSP_054731;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal liver; less expressed in
CC fetal brain, lung, and kidney. At the adult stage, expression is
CC drastically reduced in the liver but highly expressed in the spleen,
CC brain, lung, lymph nodes and peripheral blood leukocytes.
CC -!- INDUCTION: Up-regulated in response to activation in primary T helper
CC cells. {ECO:0000269|PubMed:18945965}.
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DR EMBL; AF201925; AAF09255.1; -; mRNA.
DR EMBL; AF087858; AAP97168.1; -; mRNA.
DR EMBL; AF151864; AAD34101.1; -; mRNA.
DR EMBL; AF153607; AAD41089.1; -; mRNA.
DR EMBL; AF111112; AAF27195.1; -; mRNA.
DR EMBL; AF112203; AAF17191.1; -; mRNA.
DR EMBL; AK312170; BAG35104.1; -; mRNA.
DR EMBL; AC146507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471195; EAW85022.1; -; Genomic_DNA.
DR EMBL; CH471195; EAW85023.1; -; Genomic_DNA.
DR EMBL; BC000007; AAH00007.1; -; mRNA.
DR EMBL; BC007268; AAH07268.1; -; mRNA.
DR EMBL; BC008307; AAH08307.1; -; mRNA.
DR EMBL; BC008866; AAH08866.1; -; mRNA.
DR EMBL; BC013733; AAH13733.1; -; mRNA.
DR EMBL; BC013748; AAH13748.1; -; mRNA.
DR EMBL; BC078182; AAH78182.1; -; mRNA.
DR CCDS; CCDS4415.1; -. [Q9Y255-1]
DR CCDS; CCDS64328.1; -. [Q9Y255-2]
DR RefSeq; NP_001258757.1; NM_001271828.1. [Q9Y255-2]
DR RefSeq; NP_037369.1; NM_013237.3. [Q9Y255-1]
DR PDB; 6I3V; X-ray; 1.98 A; B/F=1-173.
DR PDB; 6I3Y; X-ray; 2.98 A; C/F=1-173.
DR PDBsum; 6I3V; -.
DR PDBsum; 6I3Y; -.
DR AlphaFoldDB; Q9Y255; -.
DR SMR; Q9Y255; -.
DR BioGRID; 118045; 36.
DR IntAct; Q9Y255; 10.
DR STRING; 9606.ENSP00000302114; -.
DR GlyGen; Q9Y255; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y255; -.
DR PhosphoSitePlus; Q9Y255; -.
DR BioMuta; PRELID1; -.
DR DMDM; 29839690; -.
DR EPD; Q9Y255; -.
DR jPOST; Q9Y255; -.
DR MassIVE; Q9Y255; -.
DR MaxQB; Q9Y255; -.
DR PaxDb; Q9Y255; -.
DR PeptideAtlas; Q9Y255; -.
DR PRIDE; Q9Y255; -.
DR ProteomicsDB; 14004; -.
DR ProteomicsDB; 85657; -. [Q9Y255-1]
DR Antibodypedia; 1204; 160 antibodies from 23 providers.
DR DNASU; 27166; -.
DR Ensembl; ENST00000303204.9; ENSP00000302114.4; ENSG00000169230.10. [Q9Y255-1]
DR Ensembl; ENST00000503216.5; ENSP00000427097.1; ENSG00000169230.10. [Q9Y255-2]
DR GeneID; 27166; -.
DR KEGG; hsa:27166; -.
DR MANE-Select; ENST00000303204.9; ENSP00000302114.4; NM_013237.4; NP_037369.1.
DR UCSC; uc003mfx.5; human. [Q9Y255-1]
DR CTD; 27166; -.
DR DisGeNET; 27166; -.
DR GeneCards; PRELID1; -.
DR HGNC; HGNC:30255; PRELID1.
DR HPA; ENSG00000169230; Low tissue specificity.
DR MIM; 605733; gene.
DR neXtProt; NX_Q9Y255; -.
DR OpenTargets; ENSG00000169230; -.
DR PharmGKB; PA162400040; -.
DR VEuPathDB; HostDB:ENSG00000169230; -.
DR eggNOG; KOG3337; Eukaryota.
DR GeneTree; ENSGT00950000182810; -.
DR HOGENOM; CLU_067902_3_0_1; -.
DR InParanoid; Q9Y255; -.
DR OMA; LAFFNRY; -.
DR OrthoDB; 1369397at2759; -.
DR PhylomeDB; Q9Y255; -.
DR TreeFam; TF313119; -.
DR PathwayCommons; Q9Y255; -.
DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR SignaLink; Q9Y255; -.
DR BioGRID-ORCS; 27166; 782 hits in 1089 CRISPR screens.
DR ChiTaRS; PRELID1; human.
DR GenomeRNAi; 27166; -.
DR Pharos; Q9Y255; Tbio.
DR PRO; PR:Q9Y255; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y255; protein.
DR Bgee; ENSG00000169230; Expressed in body of pancreas and 161 other tissues.
DR ExpressionAtlas; Q9Y255; baseline and differential.
DR Genevisible; Q9Y255; HS.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0120009; P:intermembrane lipid transfer; IEA:GOC.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IDA:UniProtKB.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IDA:UniProtKB.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IDA:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; IDA:UniProtKB.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0097035; P:regulation of membrane lipid distribution; IDA:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:UniProtKB.
DR GO; GO:0045580; P:regulation of T cell differentiation; IDA:UniProtKB.
DR InterPro; IPR006797; PRELI/MSF1_dom.
DR InterPro; IPR037365; Slowmo/Ups.
DR PANTHER; PTHR11158; PTHR11158; 1.
DR Pfam; PF04707; PRELI; 1.
DR PROSITE; PS50904; PRELI_MSF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Lipid transport;
KW Mitochondrion; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:14640972"
FT CHAIN ?..219
FT /note="PRELI domain-containing protein 1, mitochondrial"
FT /id="PRO_0000097119"
FT DOMAIN 36..174
FT /note="PRELI/MSF1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00158"
FT VAR_SEQ 171..181
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_054731"
FT CONFLICT 127
FT /note="R -> H (in Ref. 1; AAF09255)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> T (in Ref. 6; AAF17191)"
FT /evidence="ECO:0000305"
FT STRAND 1..13
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:6I3V"
FT STRAND 34..44
FT /evidence="ECO:0007829|PDB:6I3V"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6I3V"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6I3Y"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6I3V"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:6I3V"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6I3V"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:6I3V"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 136..169
FT /evidence="ECO:0007829|PDB:6I3V"
SQ SEQUENCE 219 AA; 25181 MW; CCDBF54FA573509F CRC64;
MVKYFLGQSV LRSSWDQVFA AFWQRYPNPY SKHVLTEDIV HREVTPDQKL LSRRLLTKTN
RMPRWAERLF PANVAHSVYV LEDSIVDPQN QTMTTFTWNI NHARLMVVEE RCVYCVNSDN
SGWTEIRREA WVSSSLFGVS RAVQEFGLAR FKSNVTKTMK GFEYILAKLQ GEAPSKTLVE
TAKEAKEKAK ETALAATEKA KDLASKAATK KQQQQQQFV
