AZI2_HUMAN
ID AZI2_HUMAN Reviewed; 392 AA.
AC Q9H6S1; A8K3M2; C9JB40; H7BXU6; Q86W99; Q9BQF1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=5-azacytidine-induced protein 2;
DE AltName: Full=NF-kappa-B-activating kinase-associated protein 1 {ECO:0000303|PubMed:14560022};
DE Short=Nak-associated protein 1 {ECO:0000303|PubMed:14560022};
DE Short=Nap1 {ECO:0000303|PubMed:14560022};
DE AltName: Full=TILP {ECO:0000303|Ref.2};
GN Name=AZI2; Synonyms=NAP1 {ECO:0000303|PubMed:14560022}, TBKBP2;
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), FUNCTION, INTERACTION WITH TBK1 AND
RP IKBKE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14560022; DOI=10.1128/mcb.23.21.7780-7793.2003;
RA Fujita F., Taniguchi Y., Kato T., Narita Y., Furuya A., Ogawa T.,
RA Sakurai H., Joh T., Itoh M., Delhase M., Karin M., Nakanishi M.;
RT "Identification of NAP1, a regulatory subunit of IkappaB kinase-related
RT kinases that potentiates NF-kappaB signaling.";
RL Mol. Cell. Biol. 23:7780-7793(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RA Inohara N., Koseki T., Nunez G.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo, and Hepatoma;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH TICAM1.
RX PubMed=15611223; DOI=10.4049/jimmunol.174.1.27;
RA Sasai M., Oshiumi H., Matsumoto M., Inoue N., Fujita F., Nakanishi M.,
RA Seya T.;
RT "NF-kappaB-activating kinase-associated protein 1 participates in
RT TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN
RT regulatory factor 3 activation.";
RL J. Immunol. 174:27-30(2005).
RN [7]
RP INTERACTION WITH IKBKE.
RX PubMed=17568778; DOI=10.1038/sj.emboj.7601743;
RA Ryzhakov G., Randow F.;
RT "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-
RT binding domain with NAP1 and TANK.";
RL EMBO J. 26:3180-3190(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, 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-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH TBK1.
RX PubMed=21931631; DOI=10.1371/journal.pone.0023971;
RA Goncalves A., Burckstummer T., Dixit E., Scheicher R., Gorna M.W.,
RA Karayel E., Sugar C., Stukalov A., Berg T., Kralovics R., Planyavsky M.,
RA Bennett K.L., Colinge J., Superti-Furga G.;
RT "Functional dissection of the TBK1 molecular network.";
RL PLoS ONE 6:E23971-E23971(2011).
RN [11]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN C6.
RX PubMed=21931555; DOI=10.1371/journal.ppat.1002247;
RA Unterholzner L., Sumner R.P., Baran M., Ren H., Mansur D.S., Bourke N.M.,
RA Randow F., Smith G.L., Bowie A.G.;
RT "Vaccinia virus protein C6 is a virulence factor that binds TBK-1 adaptor
RT proteins and inhibits activation of IRF3 and IRF7.";
RL PLoS Pathog. 7:E1002247-E1002247(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
RP INTERACTION WITH TBK1.
RX PubMed=29251827; DOI=10.1002/pmic.201700403;
RA Shang J., Xia T., Han Q.Q., Zhao X., Hu M.M., Shu H.B., Guo L.;
RT "Quantitative Proteomics Identified TTC4 as a TBK1 Interactor and a
RT Positive Regulator of SeV-Induced Innate Immunity.";
RL Proteomics 18:0-0(2018).
CC -!- FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in
CC antiviral innate immunity (PubMed:14560022, PubMed:21931631). Activates
CC serine/threonine-protein kinase TBK1 and facilitates its
CC oligomerization (PubMed:14560022, PubMed:21931631). Enhances the
CC phosphorylation of NF-kappa-B p65 subunit RELA by TBK1
CC (PubMed:14560022, PubMed:21931631). Promotes TBK1-induced as well as
CC TNF-alpha or PMA-induced activation of NF-kappa-B (PubMed:14560022,
CC PubMed:21931631). Participates in IFNB promoter activation via TICAM1
CC (PubMed:15611223). {ECO:0000269|PubMed:14560022,
CC ECO:0000269|PubMed:15611223, ECO:0000269|PubMed:21931631}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with IKBKE
CC (PubMed:14560022, PubMed:17568778). Interacts with TBK1
CC (PubMed:14560022, PubMed:21931631, PubMed:29251827). Interacts with
CC TICAM1 (PubMed:15611223). {ECO:0000250|UniProtKB:Q9QYP6,
CC ECO:0000269|PubMed:14560022, ECO:0000269|PubMed:15611223,
CC ECO:0000269|PubMed:17568778, ECO:0000269|PubMed:21931631,
CC ECO:0000269|PubMed:29251827}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein C6
CC (PubMed:21931555). {ECO:0000269|PubMed:21931555}.
CC -!- INTERACTION:
CC Q9H6S1; Q9UHD2: TBK1; NbExp=7; IntAct=EBI-359973, EBI-356402;
CC Q9H6S1; P17362: VACWR022; Xeno; NbExp=2; IntAct=EBI-359973, EBI-9519257;
CC Q9H6S1; Q9E7P0; Xeno; NbExp=2; IntAct=EBI-359973, EBI-11361108;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14560022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long;
CC IsoId=Q9H6S1-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9H6S1-3; Sequence=VSP_023817, VSP_023818;
CC Name=3;
CC IsoId=Q9H6S1-4; Sequence=VSP_047087, VSP_047090;
CC Name=4;
CC IsoId=Q9H6S1-5; Sequence=VSP_047088, VSP_047089;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:14560022). Abundant
CC expression seen in the pancreas and testis (PubMed:14560022).
CC {ECO:0000269|PubMed:14560022}.
CC -!- PTM: Ubiquitinated via 'Lys-48'-linked polyubiquitination by TRIM38,
CC leading to its degradation. {ECO:0000250|UniProtKB:Q9QYP6}.
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DR EMBL; AY151386; AAO05967.1; -; mRNA.
DR EMBL; AF044917; AAF22368.1; -; Genomic_DNA.
DR EMBL; AF044918; AAF22369.1; -; Genomic_DNA.
DR EMBL; AK025592; BAB15182.1; -; mRNA.
DR EMBL; AK290637; BAF83326.1; -; mRNA.
DR EMBL; AC092503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64395.1; -; Genomic_DNA.
DR CCDS; CCDS2647.1; -. [Q9H6S1-1]
DR CCDS; CCDS46782.1; -. [Q9H6S1-4]
DR CCDS; CCDS46783.1; -. [Q9H6S1-5]
DR RefSeq; NP_001127904.1; NM_001134432.1. [Q9H6S1-4]
DR RefSeq; NP_001127905.1; NM_001134433.1. [Q9H6S1-5]
DR RefSeq; NP_071906.1; NM_022461.4. [Q9H6S1-1]
DR RefSeq; XP_005265449.1; XM_005265392.2. [Q9H6S1-1]
DR PDB; 5EP6; X-ray; 1.45 A; A/C=215-255.
DR PDB; 5Z7G; X-ray; 2.30 A; C/D=33-75.
DR PDB; 5Z7L; X-ray; 2.02 A; C/D=33-75.
DR PDB; 7EA2; X-ray; 2.14 A; A/B=6-16.
DR PDBsum; 5EP6; -.
DR PDBsum; 5Z7G; -.
DR PDBsum; 5Z7L; -.
DR PDBsum; 7EA2; -.
DR AlphaFoldDB; Q9H6S1; -.
DR SMR; Q9H6S1; -.
DR BioGRID; 122142; 33.
DR ComplexPortal; CPX-6038; TBK1-IKKepsilon-NAP1 complex.
DR CORUM; Q9H6S1; -.
DR DIP; DIP-27605N; -.
DR IntAct; Q9H6S1; 15.
DR MINT; Q9H6S1; -.
DR STRING; 9606.ENSP00000419371; -.
DR ChEMBL; CHEMBL4523456; -.
DR iPTMnet; Q9H6S1; -.
DR MetOSite; Q9H6S1; -.
DR PhosphoSitePlus; Q9H6S1; -.
DR BioMuta; AZI2; -.
DR DMDM; 74718550; -.
DR EPD; Q9H6S1; -.
DR jPOST; Q9H6S1; -.
DR MassIVE; Q9H6S1; -.
DR MaxQB; Q9H6S1; -.
DR PaxDb; Q9H6S1; -.
DR PeptideAtlas; Q9H6S1; -.
DR PRIDE; Q9H6S1; -.
DR ProteomicsDB; 43401; -.
DR ProteomicsDB; 81026; -. [Q9H6S1-1]
DR ProteomicsDB; 81027; -. [Q9H6S1-3]
DR ProteomicsDB; 9412; -.
DR Antibodypedia; 27537; 135 antibodies from 23 providers.
DR DNASU; 64343; -.
DR Ensembl; ENST00000334100.10; ENSP00000335609.6; ENSG00000163512.14. [Q9H6S1-5]
DR Ensembl; ENST00000420543.6; ENSP00000391696.2; ENSG00000163512.14. [Q9H6S1-4]
DR Ensembl; ENST00000457172.5; ENSP00000389577.1; ENSG00000163512.14. [Q9H6S1-4]
DR Ensembl; ENST00000479665.6; ENSP00000419371.1; ENSG00000163512.14. [Q9H6S1-1]
DR GeneID; 64343; -.
DR KEGG; hsa:64343; -.
DR MANE-Select; ENST00000479665.6; ENSP00000419371.1; NM_022461.5; NP_071906.1.
DR UCSC; uc003ceb.5; human. [Q9H6S1-1]
DR CTD; 64343; -.
DR DisGeNET; 64343; -.
DR GeneCards; AZI2; -.
DR HGNC; HGNC:24002; AZI2.
DR HPA; ENSG00000163512; Low tissue specificity.
DR MIM; 609916; gene.
DR neXtProt; NX_Q9H6S1; -.
DR OpenTargets; ENSG00000163512; -.
DR PharmGKB; PA134950985; -.
DR VEuPathDB; HostDB:ENSG00000163512; -.
DR eggNOG; ENOG502QV07; Eukaryota.
DR GeneTree; ENSGT00940000153704; -.
DR InParanoid; Q9H6S1; -.
DR OMA; PWPSQSC; -.
DR OrthoDB; 1268120at2759; -.
DR PhylomeDB; Q9H6S1; -.
DR TreeFam; TF331289; -.
DR PathwayCommons; Q9H6S1; -.
DR SignaLink; Q9H6S1; -.
DR BioGRID-ORCS; 64343; 49 hits in 1074 CRISPR screens.
DR ChiTaRS; AZI2; human.
DR GeneWiki; AZI2; -.
DR GenomeRNAi; 64343; -.
DR Pharos; Q9H6S1; Tbio.
DR PRO; PR:Q9H6S1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H6S1; protein.
DR Bgee; ENSG00000163512; Expressed in stromal cell of endometrium and 194 other tissues.
DR ExpressionAtlas; Q9H6S1; baseline and differential.
DR Genevisible; Q9H6S1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IC:ComplexPortal.
DR GO; GO:0051607; P:defense response to virus; IC:ComplexPortal.
DR GO; GO:0097028; P:dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0044565; P:dendritic cell proliferation; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0042110; P:T cell activation; IEA:Ensembl.
DR GO; GO:0060337; P:type I interferon signaling pathway; IC:ComplexPortal.
DR InterPro; IPR024581; TBD.
DR Pfam; PF12845; TBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Host-virus interaction; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..392
FT /note="5-azacytidine-induced protein 2"
FT /id="PRO_0000280602"
FT REGION 1..197
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9QYP6"
FT REGION 216..257
FT /note="Interaction with TBK1 and IKBKE"
FT /evidence="ECO:0000269|PubMed:14560022"
FT COILED 40..76
FT /evidence="ECO:0000255"
FT COILED 102..196
FT /evidence="ECO:0000255"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMA0"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 216..243
FT /note="SDNMQHAYWELKREMSNLHLVTQVQAEL -> RQSICSTAWSAVAQSWDSMN
FT FEDCSLFA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047087"
FT VAR_SEQ 216..232
FT /note="SDNMQHAYWELKREMSN -> RVSVAQPGVQWRNHGIA (in isoform
FT 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047088"
FT VAR_SEQ 216..228
FT /note="SDNMQHAYWELKR -> TQPGVQWRNHGIA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_023817"
FT VAR_SEQ 229..392
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_023818"
FT VAR_SEQ 233..392
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047089"
FT VAR_SEQ 244..392
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047090"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:7EA2"
FT HELIX 34..72
FT /evidence="ECO:0007829|PDB:5Z7L"
FT HELIX 216..246
FT /evidence="ECO:0007829|PDB:5EP6"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5EP6"
SQ SEQUENCE 392 AA; 44935 MW; EFDBDDA60C5CD624 CRC64;
MDALVEDDIC ILNHEKAHKR DTVTPVSIYS GDESVASHFA LVTAYEDIKK RLKDSEKENS
LLKKRIRFLE EKLIARFEEE TSSVGREQVN KAYHAYREVC IDRDNLKSKL DKMNKDNSES
LKVLNEQLQS KEVELLQLRT EVETQQVMRN LNPPSSNWEV EKLSCDLKIH GLEQELELMR
KECSDLKIEL QKAKQTDPYQ EDNLKSRDLQ KLSISSDNMQ HAYWELKREM SNLHLVTQVQ
AELLRKLKTS TAIKKACAPV GCSEDLGRDS TKLHLMNFTA TYTRHPPLLP NGKALCHTTS
SPLPGDVKVL SEKAILQSWT DNERSIPNDG TCFQEHSSYG RNSLEDNSWV FPSPPKSSET
AFGETKTKTL PLPNLPPLHY LDQHNQNCLY KN
