ZNHI3_HUMAN
ID ZNHI3_HUMAN Reviewed; 155 AA.
AC Q15649; A8K493; K7EQP1; Q8WVJ3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Zinc finger HIT domain-containing protein 3;
DE AltName: Full=HNF-4a coactivator;
DE AltName: Full=Thyroid hormone receptor interactor 3;
DE AltName: Full=Thyroid receptor-interacting protein 3;
DE Short=TR-interacting protein 3;
DE Short=TRIP-3;
GN Name=ZNHIT3; Synonyms=TRIP3;
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].
RX PubMed=11916906; DOI=10.2337/diabetes.51.4.910;
RA Iwahashi H., Yamagata K., Yoshiuchi I., Terasaki J., Yang Q., Fukui K.,
RA Ihara A., Zhu Q., Asakura T., Cao Y., Imagawa A., Namba M., Hanafusa T.,
RA Miyagawa J., Matsuzawa Y.;
RT "Thyroid hormone receptor interacting protein 3 (trip3) is a novel
RT coactivator of hepatocyte nuclear factor-4alpha.";
RL Diabetes 51:910-914(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-155, AND INTERACTION WITH THYROID RECEPTOR.
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP SUBCELLULAR LOCATION, INTERACTION WITH NUFIP1, INVOLVEMENT IN PEHO, VARIANT
RP PEHO LEU-31, AND CHARACTERIZATION OF VARIANT PEHO LEU-31.
RX PubMed=28335020; DOI=10.1093/brain/awx040;
RA Anttonen A.K., Laari A., Kousi M., Yang Y.J., Jaeaeskelaeinen T., Somer M.,
RA Siintola E., Jakkula E., Muona M., Tegelberg S., Loennqvist T., Pihko H.,
RA Valanne L., Paetau A., Lun M.P., Haestbacka J., Kopra O., Joensuu T.,
RA Katsanis N., Lehtinen M.K., Palvimo J.J., Lehesjoki A.E.;
RT "ZNHIT3 is defective in PEHO syndrome, a severe encephalopathy with
RT cerebellar granule neuron loss.";
RL Brain 140:1267-1279(2017).
RN [13]
RP INTERACTION WITH RUVBL1/RUVBL2 COMPLEX.
RX PubMed=28561026; DOI=10.1038/ncomms15615;
RA Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E.,
RA Bouchard A., Faubert D., Chabot B., Coulombe B.;
RT "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2
RT to regulate assembly of U5 small nuclear ribonucleoprotein.";
RL Nat. Commun. 8:15615-15615(2017).
RN [14]
RP STRUCTURE BY NMR OF 1-46.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-HIT domain in zinc finger HIT domain-
RT containing protein 3 (TRIP-3).";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- SUBUNIT: Thyroid receptor interacting proteins (TRIPs) specifically
CC interact with the ligand binding domain of the thyroid receptor (TR)
CC (PubMed:7776974). Requires the presence of thyroid hormone for its
CC interaction (PubMed:7776974). Interacts with NUFIP1 (PubMed:28335020).
CC Interacts (via HIT-type zinc finger) with the RUVBL1/RUVBL2 complex in
CC the presence of ADP (PubMed:28561026). {ECO:0000269|PubMed:28335020,
CC ECO:0000269|PubMed:28561026}.
CC -!- INTERACTION:
CC Q15649; Q9UHK0: NUFIP1; NbExp=7; IntAct=EBI-2563564, EBI-2563549;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28335020}. Nucleus
CC {ECO:0000269|PubMed:28335020}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15649-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15649-2; Sequence=VSP_055155;
CC -!- DISEASE: PEHO syndrome (PEHO) [MIM:260565]: An autosomal recessive
CC syndrome characterized by progressive encephalopathy, lack of
CC psychomotor development, severe intellectual disability, early onset
CC epileptic seizures, optic nerve/cerebellar atrophy, pedal edema, and
CC early death. {ECO:0000269|PubMed:28335020}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
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DR EMBL; AF400652; AAM82423.1; -; mRNA.
DR EMBL; AK290858; BAF83547.1; -; mRNA.
DR EMBL; AC126327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471199; EAW57552.1; -; Genomic_DNA.
DR EMBL; BC017931; AAH17931.1; -; mRNA.
DR EMBL; L40410; AAC41737.1; -; mRNA.
DR CCDS; CCDS11312.1; -. [Q15649-1]
DR CCDS; CCDS62156.1; -. [Q15649-2]
DR RefSeq; NP_001268361.1; NM_001281432.1. [Q15649-2]
DR RefSeq; NP_001268362.1; NM_001281433.1.
DR RefSeq; NP_001268363.1; NM_001281434.1.
DR RefSeq; NP_004764.1; NM_004773.3. [Q15649-1]
DR PDB; 2YQQ; NMR; -; A=4-46.
DR PDB; 5L85; NMR; -; A=85-155.
DR PDBsum; 2YQQ; -.
DR PDBsum; 5L85; -.
DR AlphaFoldDB; Q15649; -.
DR SMR; Q15649; -.
DR BioGRID; 114736; 50.
DR IntAct; Q15649; 21.
DR STRING; 9606.ENSP00000484687; -.
DR iPTMnet; Q15649; -.
DR PhosphoSitePlus; Q15649; -.
DR BioMuta; ZNHIT3; -.
DR DMDM; 46397898; -.
DR EPD; Q15649; -.
DR jPOST; Q15649; -.
DR MassIVE; Q15649; -.
DR MaxQB; Q15649; -.
DR PaxDb; Q15649; -.
DR PeptideAtlas; Q15649; -.
DR PRIDE; Q15649; -.
DR ProteomicsDB; 60687; -. [Q15649-1]
DR Antibodypedia; 74086; 55 antibodies from 19 providers.
DR DNASU; 9326; -.
DR Ensembl; ENST00000617429.5; ENSP00000484687.1; ENSG00000273611.5. [Q15649-1]
DR Ensembl; ENST00000619649.4; ENSP00000478183.1; ENSG00000278574.4. [Q15649-2]
DR Ensembl; ENST00000620324.4; ENSP00000479727.1; ENSG00000273611.5. [Q15649-2]
DR Ensembl; ENST00000620508.4; ENSP00000481504.1; ENSG00000278574.4. [Q15649-1]
DR GeneID; 9326; -.
DR KEGG; hsa:9326; -.
DR MANE-Select; ENST00000617429.5; ENSP00000484687.1; NM_004773.4; NP_004764.1.
DR UCSC; uc002hms.3; human. [Q15649-1]
DR CTD; 9326; -.
DR DisGeNET; 9326; -.
DR GeneCards; ZNHIT3; -.
DR HGNC; HGNC:12309; ZNHIT3.
DR HPA; ENSG00000273611; Low tissue specificity.
DR MalaCards; ZNHIT3; -.
DR MIM; 260565; phenotype.
DR MIM; 604500; gene.
DR neXtProt; NX_Q15649; -.
DR OpenTargets; ENSG00000273611; -.
DR Orphanet; 2836; PEHO syndrome.
DR PharmGKB; PA36987; -.
DR VEuPathDB; HostDB:ENSG00000273611; -.
DR eggNOG; KOG2857; Eukaryota.
DR GeneTree; ENSGT00390000010822; -.
DR HOGENOM; CLU_117355_1_0_1; -.
DR InParanoid; Q15649; -.
DR OMA; EAQSKYK; -.
DR PhylomeDB; Q15649; -.
DR TreeFam; TF324673; -.
DR PathwayCommons; Q15649; -.
DR SignaLink; Q15649; -.
DR BioGRID-ORCS; 9326; 421 hits in 1076 CRISPR screens.
DR ChiTaRS; ZNHIT3; human.
DR EvolutionaryTrace; Q15649; -.
DR GenomeRNAi; 9326; -.
DR Pharos; Q15649; Tbio.
DR PRO; PR:Q15649; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q15649; protein.
DR Bgee; ENSG00000273611; Expressed in cortical plate and 101 other tissues.
DR ExpressionAtlas; Q15649; baseline and differential.
DR Genevisible; Q15649; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070761; C:pre-snoRNP complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; TAS:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0048254; P:snoRNA localization; IBA:GO_Central.
DR InterPro; IPR007529; Znf_HIT.
DR InterPro; IPR040197; ZNHIT3.
DR PANTHER; PTHR13483:SF11; PTHR13483:SF11; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Epilepsy;
KW Intellectual disability; Metal-binding; Neurodegeneration; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..155
FT /note="Zinc finger HIT domain-containing protein 3"
FT /id="PRO_0000173550"
FT ZN_FING 11..42
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 96..155
FT /note="GESATLRSLLLNPHLRQLMVNLDQGEDKAKLMRAYMQEPLFVEFADCCLGIV
FT EPSQNEES -> DGLSSCHPGWSAAAQSRLTATSPSQIQAILMPQPPEQLGLQAPATTP
FT NQFLYF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055155"
FT VARIANT 31
FT /note="S -> L (in PEHO; increased protein degradation;
FT decreased protein abundance; does not affect localization
FT to cytoplasm and nucleus; dbSNP:rs148890852)"
FT /evidence="ECO:0000269|PubMed:28335020"
FT /id="VAR_079193"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2YQQ"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2YQQ"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2YQQ"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2YQQ"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:2YQQ"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:5L85"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5L85"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:5L85"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:5L85"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:5L85"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5L85"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:5L85"
SQ SEQUENCE 155 AA; 17607 MW; A115FD0AA9321AB0 CRC64;
MASLKCSTVV CVICLEKPKY RCPACRVPYC SVVCFRKHKE QCNPETRPVE KKIRSALPTK
TVKPVENKDD DDSIADFLNS DEEEDRVSLQ NLKNLGESAT LRSLLLNPHL RQLMVNLDQG
EDKAKLMRAY MQEPLFVEFA DCCLGIVEPS QNEES
