ID   PPIL3_HUMAN             Reviewed;         161 AA.
AC   Q9H2H8; Q86WF9; Q96IA9; Q9BXZ1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 3;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin J;
DE            Short=CyPJ;
DE   AltName: Full=Cyclophilin-like protein PPIL3;
DE   AltName: Full=Rotamase PPIL3;
GN   Name=PPIL3;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=11435694; DOI=10.1159/000056909;
RA   Zhou Z., Ying K., Dai J., Tang R., Wang W., Huang Y., Zhao W., Xie Y.,
RA   Mao Y.;
RT   "Molecular cloning and characterization of a novel peptidylprolyl isomerase
RT   (cyclophilin)-like gene (PPIL3) from human fetal brain.";
RL   Cytogenet. Cell Genet. 92:231-236(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ding J.B., Yu L., Zhao S.Y.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-146.
RC   TISSUE=Placenta;
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 BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP   C COMPLEX.
RX   PubMed=11991638; DOI=10.1017/s1355838202021088;
RA   Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT   "Purification and characterization of native spliceosomes suitable for
RT   three-dimensional structural analysis.";
RL   RNA 8:426-439(2002).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=15735342; DOI=10.1107/s0907444904033189;
RA   Huang L.-L., Zhao X.-M., Huang C.-Q., Yu L., Xia Z.-X.;
RT   "Structure of recombinant human cyclophilin J, a novel member of the
RT   cyclophilin family.";
RL   Acta Crystallogr. D 61:316-321(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. May be involved in pre-mRNA splicing.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBUNIT: Identified in the spliceosome C complex.
CC       {ECO:0000269|PubMed:11991638}.
CC   -!- INTERACTION:
CC       Q9H2H8; Q86UT8: CENATAC; NbExp=3; IntAct=EBI-751051, EBI-11028020;
CC       Q9H2H8; O95391: SLU7; NbExp=5; IntAct=EBI-751051, EBI-750559;
CC       Q9H2H8; Q99152: VP3; Xeno; NbExp=3; IntAct=EBI-751051, EBI-1776808;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PPIL3b;
CC         IsoId=Q9H2H8-1; Sequence=Displayed;
CC       Name=2; Synonyms=PPIL3a;
CC         IsoId=Q9H2H8-2; Sequence=VSP_015468;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Detected at low levels.
CC       {ECO:0000269|PubMed:11435694}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF251049; AAK34939.1; -; mRNA.
DR   EMBL; AF271652; AAG44766.1; -; mRNA.
DR   EMBL; AF146799; AAO64723.1; -; mRNA.
DR   EMBL; AK027315; BAB55036.1; -; mRNA.
DR   EMBL; AC005037; AAY14723.1; -; Genomic_DNA.
DR   EMBL; BC007693; AAH07693.1; -; mRNA.
DR   CCDS; CCDS2332.1; -. [Q9H2H8-2]
DR   CCDS; CCDS2333.1; -. [Q9H2H8-1]
DR   RefSeq; NP_115861.1; NM_032472.3. [Q9H2H8-2]
DR   RefSeq; NP_570981.1; NM_130906.2. [Q9H2H8-1]
DR   RefSeq; XP_005246708.1; XM_005246651.3. [Q9H2H8-2]
DR   RefSeq; XP_005246709.1; XM_005246652.4. [Q9H2H8-1]
DR   RefSeq; XP_011509660.1; XM_011511358.2. [Q9H2H8-1]
DR   RefSeq; XP_016859841.1; XM_017004352.1. [Q9H2H8-2]
DR   RefSeq; XP_016859842.1; XM_017004353.1. [Q9H2H8-2]
DR   RefSeq; XP_016859843.1; XM_017004354.1. [Q9H2H8-2]
DR   RefSeq; XP_016859844.1; XM_017004355.1. [Q9H2H8-1]
DR   RefSeq; XP_016859845.1; XM_017004356.1. [Q9H2H8-1]
DR   PDB; 1XYH; X-ray; 2.60 A; A=1-161.
DR   PDB; 2OJU; X-ray; 2.40 A; A/B=1-161.
DR   PDB; 2OK3; X-ray; 2.00 A; A=1-161.
DR   PDB; 8C6J; EM; 2.80 A; C3=1-161.
DR   PDBsum; 1XYH; -.
DR   PDBsum; 2OJU; -.
DR   PDBsum; 2OK3; -.
DR   PDBsum; 8C6J; -.
DR   AlphaFoldDB; Q9H2H8; -.
DR   EMDB; EMD-16452; -.
DR   SMR; Q9H2H8; -.
DR   BioGRID; 119820; 84.
DR   CORUM; Q9H2H8; -.
DR   IntAct; Q9H2H8; 23.
DR   MINT; Q9H2H8; -.
DR   STRING; 9606.ENSP00000286175; -.
DR   GlyGen; Q9H2H8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H2H8; -.
DR   MetOSite; Q9H2H8; -.
DR   PhosphoSitePlus; Q9H2H8; -.
DR   BioMuta; PPIL3; -.
DR   DMDM; 73921766; -.
DR   EPD; Q9H2H8; -.
DR   jPOST; Q9H2H8; -.
DR   MassIVE; Q9H2H8; -.
DR   MaxQB; Q9H2H8; -.
DR   PeptideAtlas; Q9H2H8; -.
DR   ProteomicsDB; 80550; -. [Q9H2H8-1]
DR   ProteomicsDB; 80551; -. [Q9H2H8-2]
DR   Pumba; Q9H2H8; -.
DR   TopDownProteomics; Q9H2H8-1; -. [Q9H2H8-1]
DR   Antibodypedia; 34922; 266 antibodies from 24 providers.
DR   DNASU; 53938; -.
DR   Ensembl; ENST00000286175.12; ENSP00000286175.8; ENSG00000240344.10. [Q9H2H8-2]
DR   Ensembl; ENST00000392283.9; ENSP00000376107.4; ENSG00000240344.10. [Q9H2H8-1]
DR   Ensembl; ENST00000409449.5; ENSP00000387012.1; ENSG00000240344.10. [Q9H2H8-2]
DR   GeneID; 53938; -.
DR   KEGG; hsa:53938; -.
DR   MANE-Select; ENST00000392283.9; ENSP00000376107.4; NM_130906.3; NP_570981.1.
DR   UCSC; uc002uwh.4; human. [Q9H2H8-1]
DR   AGR; HGNC:9262; -.
DR   CTD; 53938; -.
DR   DisGeNET; 53938; -.
DR   GeneCards; PPIL3; -.
DR   HGNC; HGNC:9262; PPIL3.
DR   HPA; ENSG00000240344; Low tissue specificity.
DR   MIM; 615811; gene.
DR   neXtProt; NX_Q9H2H8; -.
DR   OpenTargets; ENSG00000240344; -.
DR   PharmGKB; PA33589; -.
DR   VEuPathDB; HostDB:ENSG00000240344; -.
DR   GeneTree; ENSGT00940000153189; -.
DR   HOGENOM; CLU_012062_16_3_1; -.
DR   InParanoid; Q9H2H8; -.
DR   OMA; VPFHRVM; -.
DR   OrthoDB; 554597at2759; -.
DR   PhylomeDB; Q9H2H8; -.
DR   TreeFam; TF352224; -.
DR   BRENDA; 5.2.1.8; 2681.
DR   PathwayCommons; Q9H2H8; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; Q9H2H8; -.
DR   BioGRID-ORCS; 53938; 13 hits in 1162 CRISPR screens.
DR   ChiTaRS; PPIL3; human.
DR   EvolutionaryTrace; Q9H2H8; -.
DR   GeneWiki; PPIL3; -.
DR   GenomeRNAi; 53938; -.
DR   Pharos; Q9H2H8; Tbio.
DR   PRO; PR:Q9H2H8; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9H2H8; Protein.
DR   Bgee; ENSG00000240344; Expressed in ileal mucosa and 180 other cell types or tissues.
DR   ExpressionAtlas; Q9H2H8; baseline and differential.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd01928; Cyclophilin_PPIL3_like; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 3; 1.
DR   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   Genevisible; Q9H2H8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Isomerase; Methylation;
KW   mRNA processing; mRNA splicing; Reference proteome; Rotamase; Spliceosome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   CHAIN           2..161
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 3"
FT                   /id="PRO_0000064166"
FT   DOMAIN          2..154
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         61
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6L8"
FT   VAR_SEQ         27..58
FT                   /note="NFLALCASNYYNGCIFHRNIKGFMVQTGDPTG -> MESRCVPQAGVQWRDL
FT                   GSLQPPPPGFKQVFCLSLPR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11435694,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_015468"
FT   VARIANT         146
FT                   /note="D -> E (in dbSNP:rs7562391)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_023417"
FT   CONFLICT        61..62
FT                   /note="RG -> KR (in Ref. 2; AAO64723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="S -> V (in Ref. 2; AAO64723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="Y -> I (in Ref. 2; AAO64723)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          10..16
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   HELIX           22..33
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   TURN            34..39
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:2OJU"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   HELIX           125..132
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   TURN            138..140
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:2OK3"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:2OK3"
SQ   SEQUENCE   161 AA;  18155 MW;  5FE190D7858B07D4 CRC64;
     MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC IFHRNIKGFM VQTGDPTGTG
     RGGNSIWGKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ FFITYGKQPH LDMKYTVFGK
     VIDGLETLDE LEKLPVNEKT YRPLNDVHIK DITIHANPFA Q
//