MALD2_HUMAN
ID MALD2_HUMAN Reviewed; 558 AA.
AC Q8N4S9; A1BQX0; A1BQX1; A8KA97; Q96NM9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=MARVEL domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Tricellulin {ECO:0000303|PubMed:16365161};
GN Name=MARVELD2 {ECO:0000312|HGNC:HGNC:26401}; Synonyms=TRIC;
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 VARIANT ILE-33.
RX PubMed=16365161; DOI=10.1083/jcb.200510043;
RA Ikenouchi J., Furuse M., Furuse K., Sasaki H., Tsukita S., Tsukita S.;
RT "Tricellulin constitutes a novel barrier at tricellular contacts of
RT epithelial cells.";
RL J. Cell Biol. 171:939-945(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INVOLVEMENT IN DFNB49,
RP FUNCTION, INTERACTION WITH TJP1, AND VARIANT ILE-33.
RC TISSUE=Lung;
RX PubMed=17186462; DOI=10.1086/510022;
RA Riazuddin S., Ahmed Z.M., Fanning A.S., Lagziel A., Kitajiri S., Ramzan K.,
RA Khan S.N., Chattaraj P., Friedman P.L., Anderson J.M., Belyantseva I.A.,
RA Forge A., Riazuddin S., Friedman T.B.;
RT "Tricellulin is a tight-junction protein necessary for hearing.";
RL Am. J. Hum. Genet. 79:1040-1051(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-33.
RC TISSUE=Brain, and Trachea;
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], AND VARIANT ILE-33.
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-33.
RC TISSUE=Lung;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-120, AND
RP IDENTIFICATION BY 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 IDENTIFICATION BY 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-116 AND SER-120, AND
RP IDENTIFICATION BY 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-161; THR-166 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 UBIQUITINATION, AND INTERACTION WITH ITCH.
RX PubMed=28436082; DOI=10.1111/nyas.13349;
RA Jennek S., Mittag S., Reiche J., Westphal J.K., Seelk S., Doerfel M.J.,
RA Pfirrmann T., Friedrich K., Schuetz A., Heinemann U., Huber O.;
RT "Tricellulin is a target of the ubiquitin ligase Itch.";
RL Ann. N. Y. Acad. Sci. 1397:157-168(2017).
RN [12] {ECO:0007744|PDB:5N7H, ECO:0007744|PDB:5N7I, ECO:0007744|PDB:5N7K}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 439-551, SUBCELLULAR LOCATION,
RP INTERACTION WITH TJP1, AND COILED COIL.
RX PubMed=28661558; DOI=10.1111/nyas.13408;
RA Schuetz A., Radusheva V., Krug S.M., Heinemann U.;
RT "Crystal structure of the tricellulin C-terminal coiled-coil domain reveals
RT a unique mode of dimerization.";
RL Ann. N. Y. Acad. Sci. 1405:147-159(2017).
CC -!- FUNCTION: Plays a role in the formation of tricellular tight junctions
CC and of epithelial barriers (By similarity). Required for normal hearing
CC via its role in the separation of the endolymphatic and perilymphatic
CC spaces of the organ of Corti in the inner ear, and for normal survival
CC of hair cells in the organ of Corti (PubMed:17186462).
CC {ECO:0000250|UniProtKB:Q3UZP0, ECO:0000269|PubMed:17186462}.
CC -!- SUBUNIT: Interacts with TJP1 (PubMed:17186462). Interacts with the
CC ubiquitin ligase ITCH (PubMed:28436082). Interacts (via C-terminal
CC cytoplasmic domain) with LSR (via the cytoplasmic domain), ILDR1 and
CC ILDR2; the interaction is required to recruit MARVELD2 to tricellular
CC contacts (By similarity). {ECO:0000250|UniProtKB:Q3UZP0,
CC ECO:0000269|PubMed:17186462, ECO:0000269|PubMed:28436082}.
CC -!- INTERACTION:
CC Q8N4S9; Q969F0: FATE1; NbExp=3; IntAct=EBI-6875061, EBI-743099;
CC Q8N4S9; P00747: PLG; NbExp=2; IntAct=EBI-6875061, EBI-999394;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28661558};
CC Multi-pass membrane protein {ECO:0000305}. Cell junction, tight
CC junction {ECO:0000269|PubMed:28661558}. Note=Located at tricellular
CC contacts. {ECO:0000269|PubMed:28661558}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A, TRIC;
CC IsoId=Q8N4S9-1; Sequence=Displayed;
CC Name=2; Synonyms=TRICbeta;
CC IsoId=Q8N4S9-2; Sequence=VSP_022320, VSP_022321;
CC Name=3; Synonyms=A1;
CC IsoId=Q8N4S9-3; Sequence=VSP_035760;
CC -!- PTM: Ubiquitinated by ITCH; but this ubiquitination does not lead to
CC proteasomal degradation. {ECO:0000269|PubMed:28436082}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q3UZP0}.
CC -!- DISEASE: Deafness, autosomal recessive, 49 (DFNB49) [MIM:610153]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:17186462}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01324}.
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DR EMBL; AB219936; BAE54513.1; -; mRNA.
DR EMBL; AB219937; BAE54514.1; -; mRNA.
DR EMBL; DQ682656; ABG89104.1; -; mRNA.
DR EMBL; DQ682657; ABG89105.1; -; mRNA.
DR EMBL; AK055094; BAB70853.1; -; mRNA.
DR EMBL; AK292962; BAF85651.1; -; mRNA.
DR EMBL; AC145146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471137; EAW51277.1; -; Genomic_DNA.
DR EMBL; BC033689; AAH33689.1; -; mRNA.
DR CCDS; CCDS34175.1; -. [Q8N4S9-1]
DR CCDS; CCDS58956.1; -. [Q8N4S9-3]
DR RefSeq; NP_001033692.2; NM_001038603.2. [Q8N4S9-1]
DR RefSeq; NP_001231663.1; NM_001244734.1. [Q8N4S9-3]
DR RefSeq; XP_005248502.1; XM_005248445.4. [Q8N4S9-1]
DR RefSeq; XP_005248503.1; XM_005248446.4. [Q8N4S9-1]
DR RefSeq; XP_005248504.1; XM_005248447.4. [Q8N4S9-3]
DR PDB; 5N7H; X-ray; 2.20 A; A=439-551.
DR PDB; 5N7I; X-ray; 2.88 A; A/B=439-551.
DR PDB; 5N7K; X-ray; 2.81 A; A/B/C/D=439-551.
DR PDBsum; 5N7H; -.
DR PDBsum; 5N7I; -.
DR PDBsum; 5N7K; -.
DR AlphaFoldDB; Q8N4S9; -.
DR SMR; Q8N4S9; -.
DR BioGRID; 127502; 60.
DR IntAct; Q8N4S9; 25.
DR MINT; Q8N4S9; -.
DR STRING; 9606.ENSP00000323264; -.
DR TCDB; 9.B.41.2.1; the occludin (occludin) family.
DR iPTMnet; Q8N4S9; -.
DR PhosphoSitePlus; Q8N4S9; -.
DR BioMuta; MARVELD2; -.
DR DMDM; 317373387; -.
DR EPD; Q8N4S9; -.
DR jPOST; Q8N4S9; -.
DR MassIVE; Q8N4S9; -.
DR MaxQB; Q8N4S9; -.
DR PaxDb; Q8N4S9; -.
DR PeptideAtlas; Q8N4S9; -.
DR PRIDE; Q8N4S9; -.
DR ProteomicsDB; 71965; -. [Q8N4S9-1]
DR ProteomicsDB; 71966; -. [Q8N4S9-2]
DR ProteomicsDB; 71967; -. [Q8N4S9-3]
DR Antibodypedia; 23961; 178 antibodies from 25 providers.
DR DNASU; 153562; -.
DR Ensembl; ENST00000325631.10; ENSP00000323264.5; ENSG00000152939.17. [Q8N4S9-1]
DR Ensembl; ENST00000454295.6; ENSP00000396244.2; ENSG00000152939.17. [Q8N4S9-3]
DR Ensembl; ENST00000614617.4; ENSP00000480044.1; ENSG00000274671.4.
DR Ensembl; ENST00000622835.4; ENSP00000480068.1; ENSG00000274671.4.
DR Ensembl; ENST00000645446.1; ENSP00000494616.1; ENSG00000152939.17. [Q8N4S9-1]
DR Ensembl; ENST00000647531.1; ENSP00000493858.1; ENSG00000152939.17. [Q8N4S9-3]
DR GeneID; 153562; -.
DR KEGG; hsa:153562; -.
DR MANE-Select; ENST00000325631.10; ENSP00000323264.5; NM_001038603.3; NP_001033692.2.
DR UCSC; uc003jwq.4; human. [Q8N4S9-1]
DR CTD; 153562; -.
DR DisGeNET; 153562; -.
DR GeneCards; MARVELD2; -.
DR GeneReviews; MARVELD2; -.
DR HGNC; HGNC:26401; MARVELD2.
DR HPA; ENSG00000152939; Tissue enhanced (thyroid).
DR MalaCards; MARVELD2; -.
DR MIM; 610153; phenotype.
DR MIM; 610572; gene.
DR neXtProt; NX_Q8N4S9; -.
DR OpenTargets; ENSG00000152939; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA134954584; -.
DR VEuPathDB; HostDB:ENSG00000152939; -.
DR eggNOG; KOG4796; Eukaryota.
DR GeneTree; ENSGT00940000155771; -.
DR HOGENOM; CLU_039176_1_0_1; -.
DR InParanoid; Q8N4S9; -.
DR OMA; YSQPYGV; -.
DR OrthoDB; 335949at2759; -.
DR PhylomeDB; Q8N4S9; -.
DR TreeFam; TF326161; -.
DR PathwayCommons; Q8N4S9; -.
DR SignaLink; Q8N4S9; -.
DR BioGRID-ORCS; 153562; 9 hits in 1061 CRISPR screens.
DR ChiTaRS; MARVELD2; human.
DR GeneWiki; MARVELD2; -.
DR GenomeRNAi; 153562; -.
DR Pharos; Q8N4S9; Tbio.
DR PRO; PR:Q8N4S9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N4S9; protein.
DR Bgee; ENSG00000152939; Expressed in islet of Langerhans and 104 other tissues.
DR ExpressionAtlas; Q8N4S9; baseline and differential.
DR Genevisible; Q8N4S9; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033010; C:paranodal junction; IEA:Ensembl.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR GO; GO:0070160; C:tight junction; IDA:UniProtKB.
DR GO; GO:0061689; C:tricellular tight junction; IDA:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR031177; MARVELD2.
DR InterPro; IPR010844; Occludin_ELL.
DR PANTHER; PTHR23288; PTHR23288; 1.
DR PANTHER; PTHR23288:SF3; PTHR23288:SF3; 1.
DR Pfam; PF01284; MARVEL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Coiled coil; Deafness; Hearing; Membrane; Non-syndromic deafness;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..558
FT /note="MARVEL domain-containing protein 2"
FT /id="PRO_0000271526"
FT TOPO_DOM 1..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 188..367
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 440..551
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..548
FT /evidence="ECO:0000269|PubMed:28661558"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 383..394
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17186462"
FT /id="VSP_035760"
FT VAR_SEQ 431..457
FT /note="GHIPKPIVMPDYVAKYPVIQTDDERER -> RPANFFVFLVEMGFHRVSQDD
FT LDLLTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16365161"
FT /id="VSP_022320"
FT VAR_SEQ 458..558
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16365161"
FT /id="VSP_022321"
FT VARIANT 33
FT /note="T -> I (in dbSNP:rs1185246)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15372022, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16365161, ECO:0000269|PubMed:17186462"
FT /id="VAR_047436"
FT CONFLICT 356
FT /note="L -> P (in Ref. 3; BAF85651)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="K -> R (in Ref. 3; BAF85651)"
FT /evidence="ECO:0000305"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:5N7H"
FT HELIX 452..487
FT /evidence="ECO:0007829|PDB:5N7H"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:5N7K"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:5N7K"
FT HELIX 500..517
FT /evidence="ECO:0007829|PDB:5N7H"
FT HELIX 520..549
FT /evidence="ECO:0007829|PDB:5N7H"
SQ SEQUENCE 558 AA; 64168 MW; 04F3FCB2CFDB162B CRC64;
MSNDGRSRNR DRRYDEVPSD LPYQDTTIRT HPTLHDSERA VSADPLPPPP LPLQPPFGPD
FYSSDTEEPA IAPDLKPVRR FVPDSWKNFF RGKKKDPEWD KPVSDIRYIS DGVECSPPAS
PARPNHRSPL NSCKDPYGGS EGTFSSRKEA DAVFPRDPYG SLDRHTQTVR TYSEKVEEYN
LRYSYMKSWA GLLRILGVVE LLLGAGVFAC VTAYIHKDSE WYNLFGYSQP YGMGGVGGLG
SMYGGYYYTG PKTPFVLVVA GLAWITTIII LVLGMSMYYR TILLDSNWWP LTEFGINVAL
FILYMAAAIV YVNDTNRGGL CYYPLFNTPV NAVFCRVEGG QIAAMIFLFV TMIVYLISAL
VCLKLWRHEA ARRHREYMEQ QEINEPSLSS KRKMCEMATS GDRQRDSEVN FKELRTAKMK
PELLSGHIPP GHIPKPIVMP DYVAKYPVIQ TDDERERYKA VFQDQFSEYK ELSAEVQAVL
RKFDELDAVM SRLPHHSESR QEHERISRIH EEFKKKKNDP TFLEKKERCD YLKNKLSHIK
QRIQEYDKVM NWDVQGYS
