NF2IP_HUMAN
ID NF2IP_HUMAN Reviewed; 419 AA.
AC Q8NCF5; B7Z4G5; Q66K34; Q6NVK1; Q8NFR2; Q96ST9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=NFATC2-interacting protein;
DE AltName: Full=45 kDa NF-AT-interacting protein;
DE Short=45 kDa NFAT-interacting protein;
DE AltName: Full=Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein;
GN Name=NFATC2IP; Synonyms=NIP45;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Guo J.H., Zan Q., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Eye, and Liver;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-198; SER-201;
RP SER-204 AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-220; SER-314;
RP THR-318 AND SER-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND SER-369, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-201; SER-204;
RP SER-314; SER-369 AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129 AND LYS-131, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP STRUCTURE BY NMR OF 244-419.
RG Northeast structural genomics consortium (NESG);
RT "Human NFATC2IP ubiquitin-like domains.";
RL Submitted (DEC-2010) to the PDB data bank.
CC -!- FUNCTION: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-
CC driven transcription of a specific subset of cytokine genes, including
CC IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4
CC promoter; this leads to enhancement of histone H4 'Arg-3'-methylation
CC and facilitates subsequent histone acetylation at the IL4 locus, thus
CC promotes robust cytokine expression (By similarity). Down-regulates
CC formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NFATC2, TRAF1, TRAF2 and PRMT1. Interacts with
CC UBE2I/UBC9 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8NCF5-2; Q6P5X5: C22orf39; NbExp=5; IntAct=EBI-12305293, EBI-7317823;
CC Q8NCF5-2; P27797: CALR; NbExp=3; IntAct=EBI-12305293, EBI-1049597;
CC Q8NCF5-2; Q569K6: CCDC157; NbExp=3; IntAct=EBI-12305293, EBI-13289565;
CC Q8NCF5-2; P36957: DLST; NbExp=3; IntAct=EBI-12305293, EBI-351007;
CC Q8NCF5-2; O96015: DNAL4; NbExp=6; IntAct=EBI-12305293, EBI-742362;
CC Q8NCF5-2; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-12305293, EBI-1055945;
CC Q8NCF5-2; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-12305293, EBI-3917542;
CC Q8NCF5-2; P62308: SNRPG; NbExp=3; IntAct=EBI-12305293, EBI-624585;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm
CC and prevents its translocation to the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NCF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NCF5-2; Sequence=VSP_023932;
CC Name=3;
CC IsoId=Q8NCF5-3; Sequence=VSP_023931;
CC -!- PTM: Methylation at the N-terminus by PRMT1 modulates interaction with
CC the NFAT complex and results in augmented cytokine production.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM49721.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK027545; BAB55189.1; -; mRNA.
DR EMBL; AK074761; BAC11189.1; -; mRNA.
DR EMBL; AK297333; BAH12551.1; -; mRNA.
DR EMBL; AK316535; BAH14906.1; -; mRNA.
DR EMBL; AF458593; AAM49721.1; ALT_FRAME; mRNA.
DR EMBL; BC018311; AAH18311.2; -; mRNA.
DR EMBL; BC021551; AAH21551.2; -; mRNA.
DR EMBL; BC068007; AAH68007.1; -; mRNA.
DR EMBL; BC080628; AAH80628.1; -; mRNA.
DR EMBL; BC101741; AAI01742.1; -; mRNA.
DR EMBL; BC112182; AAI12183.1; -; mRNA.
DR CCDS; CCDS10645.1; -. [Q8NCF5-1]
DR RefSeq; NP_116204.3; NM_032815.3. [Q8NCF5-1]
DR PDB; 2JXX; NMR; -; A=342-419.
DR PDB; 2L76; NMR; -; A=244-338.
DR PDB; 3RD2; X-ray; 1.60 A; A=345-419.
DR PDBsum; 2JXX; -.
DR PDBsum; 2L76; -.
DR PDBsum; 3RD2; -.
DR AlphaFoldDB; Q8NCF5; -.
DR BMRB; Q8NCF5; -.
DR SMR; Q8NCF5; -.
DR BioGRID; 124341; 55.
DR IntAct; Q8NCF5; 29.
DR MINT; Q8NCF5; -.
DR STRING; 9606.ENSP00000324792; -.
DR GlyGen; Q8NCF5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NCF5; -.
DR PhosphoSitePlus; Q8NCF5; -.
DR BioMuta; NFATC2IP; -.
DR DMDM; 74751188; -.
DR EPD; Q8NCF5; -.
DR jPOST; Q8NCF5; -.
DR MassIVE; Q8NCF5; -.
DR MaxQB; Q8NCF5; -.
DR PaxDb; Q8NCF5; -.
DR PeptideAtlas; Q8NCF5; -.
DR PRIDE; Q8NCF5; -.
DR ProteomicsDB; 72887; -. [Q8NCF5-1]
DR ProteomicsDB; 72888; -. [Q8NCF5-2]
DR ProteomicsDB; 72889; -. [Q8NCF5-3]
DR TopDownProteomics; Q8NCF5-2; -. [Q8NCF5-2]
DR Antibodypedia; 26645; 89 antibodies from 23 providers.
DR DNASU; 84901; -.
DR Ensembl; ENST00000320805.9; ENSP00000324792.4; ENSG00000176953.13. [Q8NCF5-1]
DR Ensembl; ENST00000568148.1; ENSP00000454958.1; ENSG00000176953.13. [Q8NCF5-3]
DR GeneID; 84901; -.
DR KEGG; hsa:84901; -.
DR MANE-Select; ENST00000320805.9; ENSP00000324792.4; NM_032815.4; NP_116204.3.
DR UCSC; uc002dru.4; human. [Q8NCF5-1]
DR CTD; 84901; -.
DR DisGeNET; 84901; -.
DR GeneCards; NFATC2IP; -.
DR HGNC; HGNC:25906; NFATC2IP.
DR HPA; ENSG00000176953; Low tissue specificity.
DR MIM; 614525; gene.
DR neXtProt; NX_Q8NCF5; -.
DR OpenTargets; ENSG00000176953; -.
DR PharmGKB; PA134887712; -.
DR VEuPathDB; HostDB:ENSG00000176953; -.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00390000007119; -.
DR HOGENOM; CLU_055132_1_0_1; -.
DR InParanoid; Q8NCF5; -.
DR OMA; NVVDHMA; -.
DR OrthoDB; 979809at2759; -.
DR PhylomeDB; Q8NCF5; -.
DR TreeFam; TF328600; -.
DR PathwayCommons; Q8NCF5; -.
DR SignaLink; Q8NCF5; -.
DR BioGRID-ORCS; 84901; 136 hits in 1083 CRISPR screens.
DR ChiTaRS; NFATC2IP; human.
DR EvolutionaryTrace; Q8NCF5; -.
DR GenomeRNAi; 84901; -.
DR Pharos; Q8NCF5; Tbio.
DR PRO; PR:Q8NCF5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NCF5; protein.
DR Bgee; ENSG00000176953; Expressed in trabecular bone tissue and 212 other tissues.
DR ExpressionAtlas; Q8NCF5; baseline and differential.
DR Genevisible; Q8NCF5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProt.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..419
FT /note="NFATC2-interacting protein"
FT /id="PRO_0000281008"
FT DOMAIN 348..419
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 209..231
FT /evidence="ECO:0000255"
FT COMPBIAS 89..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYG7"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09130"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09130"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09130"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..292
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023931"
FT VAR_SEQ 1..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023932"
FT VARIANT 33
FT /note="R -> W (in dbSNP:rs7201257)"
FT /id="VAR_031208"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2L76"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:2L76"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:2L76"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2L76"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:2L76"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2L76"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2L76"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:2L76"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:2L76"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:3RD2"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:3RD2"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:3RD2"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:2JXX"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:3RD2"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:3RD2"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:3RD2"
SQ SEQUENCE 419 AA; 45817 MW; CA04220B4BF0B245 CRC64;
MAEPVGKRGR WSGGSGAGRG GRGGWGGRGR RPRAQRSPSR GTLDVVSVDL VTDSDEEILE
VATARGAADE VEVEPPEPPG PVASRDNSNS DSEGEDRRPA GPPREPVRRR RRLVLDPGEA
PLVPVYSGKV KSSLRLIPDD LSLLKLYPPG DEEEAELADS SGLYHEGSPS PGSPWKTKLR
TKDKEEKKKT EFLDLDNSPL SPPSPRTKSR THTRALKKLS EVNKRLQDLR SCLSPKPPQG
QEQQGQEDEV VLVEGPTLPE TPRLFPLKIR CRADLVRLPL RMSEPLQSVV DHMATHLGVS
PSRILLLFGE TELSPTATPR TLKLGVADII DCVVLTSSPE ATETSQQLQL RVQGKEKHQT
LEVSLSRDSP LKTLMSHYEE AMGLSGRKLS FFFDGTKLSG RELPADLGME SGDLIEVWG
