ID   TCPR1_HUMAN             Reviewed;        1165 AA.
AC   Q7Z6L1; A8KAD1; B3KPZ1; C9J024; F5GX57; Q96EB0; Q9P2I9; Q9UFR6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Tectonin beta-propeller repeat-containing protein 1;
GN   Name=TECPR1; Synonyms=KIAA1358;
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 AND 3).
RC   TISSUE=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1165 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-1165 (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-938 AND SER-949, 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   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE ATG5-ATG12 CONJUGATE,
RP   AND INTERACTION WITH ATG5 AND WIPI2.
RX   PubMed=21575909; DOI=10.1016/j.chom.2011.04.010;
RA   Ogawa M., Yoshikawa Y., Kobayashi T., Mimuro H., Fukumatsu M., Kiga K.,
RA   Piao Z., Ashida H., Yoshida M., Kakuta S., Koyama T., Goto Y., Nagatake T.,
RA   Nagai S., Kiyono H., Kawalec M., Reichhart J.M., Sasakawa C.;
RT   "A Tecpr1-dependent selective autophagy pathway targets bacterial
RT   pathogens.";
RL   Cell Host Microbe 9:376-389(2011).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE ATG5-ATG12 CONJUGATE,
RP   INTERACTION WITH ATG5, AND PTDINS(3)P-BINDING.
RX   PubMed=22342342; DOI=10.1016/j.molcel.2011.12.036;
RA   Chen D., Fan W., Lu Y., Ding X., Chen S., Zhong Q.;
RT   "A mammalian autophagosome maturation mechanism mediated by TECPR1 and the
RT   Atg12-Atg5 conjugate.";
RL   Mol. Cell 45:629-641(2012).
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).
CC   -!- FUNCTION: Tethering factor involved in autophagy. Involved in
CC       autophagosome maturation by promoting the autophagosome fusion with
CC       lysosomes: acts by associating with both the ATG5-ATG12 conjugate and
CC       phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of
CC       autophagosomes. Also involved in selective autophagy against bacterial
CC       pathogens, by being required for phagophore/preautophagosomal structure
CC       biogenesis and maturation. {ECO:0000269|PubMed:21575909,
CC       ECO:0000269|PubMed:22342342}.
CC   -!- SUBUNIT: Interacts with ATG5; the interaction is direct. Interacts with
CC       WIPI2. Interacts with the ATG5-ATG12 conjugate, the interaction is
CC       however mutually exclusive with ATG16, since it does not interact with
CC       ATG12-ATG5-ATG16 complex. {ECO:0000269|PubMed:21575909,
CC       ECO:0000269|PubMed:22342342}.
CC   -!- INTERACTION:
CC       Q7Z6L1; Q9NT62: ATG3; NbExp=3; IntAct=EBI-2946676, EBI-988094;
CC       Q7Z6L1; Q9H1Y0: ATG5; NbExp=9; IntAct=EBI-2946676, EBI-1047414;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane.
CC       Lysosome membrane. Note=Localizes to Lysosome membranes, and binds
CC       PtdIns(3)P at the surface of autophagosome. Localizes to autolysosomes,
CC       a vesicle formed by the fusion between autophagosomes and lysosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q7Z6L1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z6L1-2; Sequence=VSP_033861;
CC       Name=3;
CC         IsoId=Q7Z6L1-3; Sequence=VSP_042969, VSP_042970, VSP_042973;
CC       Name=4;
CC         IsoId=Q7Z6L1-4; Sequence=VSP_042971, VSP_042972;
CC   -!- DOMAIN: The PH domain mediates the binding to phosphatidylinositol-3-
CC       phosphate (PtdIns(3)P). While full-length protein is unable to bind
CC       PtdIns(3)P in vitro, it is assumed that the binding to the ATG5-ATG12
CC       conjugate exposes the PH domain, allowing the association with
CC       PtdIns(3)P (PubMed:22342342). {ECO:0000269|PubMed:22342342}.
CC   -!- SIMILARITY: Belongs to the TECPR1 family. {ECO:0000305}.
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DR   EMBL; AK057048; BAG51853.1; -; mRNA.
DR   EMBL; AK292996; BAF85685.1; -; mRNA.
DR   EMBL; AC091654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236956; EAL23891.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76717.1; -; Genomic_DNA.
DR   EMBL; BC012529; AAH12529.2; -; mRNA.
DR   EMBL; BC053591; AAH53591.1; -; mRNA.
DR   EMBL; AB037779; BAA92596.1; -; mRNA.
DR   EMBL; AL117495; CAB55961.2; -; mRNA.
DR   CCDS; CCDS47648.1; -. [Q7Z6L1-1]
DR   PIR; T17271; T17271.
DR   RefSeq; NP_056210.1; NM_015395.2. [Q7Z6L1-1]
DR   RefSeq; XP_005250310.1; XM_005250253.3. [Q7Z6L1-1]
DR   PDB; 4TQ1; X-ray; 1.80 A; B=573-610.
DR   PDB; 8P5P; X-ray; 1.90 A; A/B/C=60-173.
DR   PDBsum; 4TQ1; -.
DR   PDBsum; 8P5P; -.
DR   AlphaFoldDB; Q7Z6L1; -.
DR   SMR; Q7Z6L1; -.
DR   BioGRID; 117375; 14.
DR   ComplexPortal; CPX-358; ATG5-ATG12-TECPR1 complex.
DR   IntAct; Q7Z6L1; 15.
DR   STRING; 9606.ENSP00000404923; -.
DR   GlyCosmos; Q7Z6L1; 1 site, 1 glycan.
DR   GlyGen; Q7Z6L1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q7Z6L1; -.
DR   PhosphoSitePlus; Q7Z6L1; -.
DR   BioMuta; TECPR1; -.
DR   DMDM; 74738829; -.
DR   EPD; Q7Z6L1; -.
DR   jPOST; Q7Z6L1; -.
DR   MassIVE; Q7Z6L1; -.
DR   MaxQB; Q7Z6L1; -.
DR   PaxDb; 9606-ENSP00000404923; -.
DR   PeptideAtlas; Q7Z6L1; -.
DR   ProteomicsDB; 69439; -. [Q7Z6L1-1]
DR   ProteomicsDB; 69440; -. [Q7Z6L1-2]
DR   ProteomicsDB; 69441; -. [Q7Z6L1-3]
DR   ProteomicsDB; 69442; -. [Q7Z6L1-4]
DR   Pumba; Q7Z6L1; -.
DR   Antibodypedia; 8742; 134 antibodies from 22 providers.
DR   DNASU; 25851; -.
DR   Ensembl; ENST00000447648.7; ENSP00000404923.2; ENSG00000205356.10. [Q7Z6L1-1]
DR   GeneID; 25851; -.
DR   KEGG; hsa:25851; -.
DR   MANE-Select; ENST00000447648.7; ENSP00000404923.2; NM_015395.3; NP_056210.1.
DR   UCSC; uc003upg.5; human. [Q7Z6L1-1]
DR   AGR; HGNC:22214; -.
DR   CTD; 25851; -.
DR   DisGeNET; 25851; -.
DR   GeneCards; TECPR1; -.
DR   HGNC; HGNC:22214; TECPR1.
DR   HPA; ENSG00000205356; Tissue enriched (pancreas).
DR   MIM; 614781; gene.
DR   neXtProt; NX_Q7Z6L1; -.
DR   OpenTargets; ENSG00000205356; -.
DR   PharmGKB; PA164726436; -.
DR   VEuPathDB; HostDB:ENSG00000205356; -.
DR   eggNOG; KOG3669; Eukaryota.
DR   GeneTree; ENSGT00510000047886; -.
DR   HOGENOM; CLU_008303_0_0_1; -.
DR   InParanoid; Q7Z6L1; -.
DR   OMA; CPMQISR; -.
DR   OrthoDB; 66441at2759; -.
DR   PhylomeDB; Q7Z6L1; -.
DR   TreeFam; TF323648; -.
DR   PathwayCommons; Q7Z6L1; -.
DR   SignaLink; Q7Z6L1; -.
DR   BioGRID-ORCS; 25851; 13 hits in 1154 CRISPR screens.
DR   ChiTaRS; TECPR1; human.
DR   GenomeRNAi; 25851; -.
DR   Pharos; Q7Z6L1; Tbio.
DR   PRO; PR:Q7Z6L1; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q7Z6L1; Protein.
DR   Bgee; ENSG00000205356; Expressed in parotid gland and 181 other cell types or tissues.
DR   ExpressionAtlas; Q7Z6L1; baseline and differential.
DR   GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0032991; C:protein-containing complex; NAS:ComplexPortal.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR   GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; IMP:ComplexPortal.
DR   GO; GO:1901096; P:regulation of autophagosome maturation; IMP:ComplexPortal.
DR   CDD; cd13300; PH1_TECPR1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR   InterPro; IPR010482; Peroxin.
DR   InterPro; IPR006614; Peroxin/Ferlin.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR23250; DYSFERLIN-RELATED; 1.
DR   PANTHER; PTHR23250:SF1; TECTONIN BETA-PROPELLER REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF06462; Hyd_WA; 4.
DR   Pfam; PF06398; Pex24p; 2.
DR   Pfam; PF19193; Tectonin; 1.
DR   SMART; SM00694; DysFC; 2.
DR   SMART; SM00693; DysFN; 2.
DR   SMART; SM00706; TECPR; 11.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   Genevisible; Q7Z6L1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autophagy; Cytoplasmic vesicle;
KW   Lipid-binding; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1165
FT                   /note="Tectonin beta-propeller repeat-containing protein 1"
FT                   /id="PRO_0000337060"
FT   REPEAT          209..240
FT                   /note="TECPR 1"
FT   REPEAT          254..285
FT                   /note="TECPR 2"
FT   REPEAT          301..332
FT                   /note="TECPR 3"
FT   REPEAT          344..376
FT                   /note="TECPR 4"
FT   DOMAIN          611..717
FT                   /note="PH"
FT   REPEAT          729..756
FT                   /note="TECPR 5"
FT   REPEAT          953..984
FT                   /note="TECPR 6"
FT   REPEAT          998..1029
FT                   /note="TECPR 7"
FT   REPEAT          1044..1075
FT                   /note="TECPR 8"
FT   REPEAT          1087..1127
FT                   /note="TECPR 9"
FT   REGION          404..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1140..1165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1140..1154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT   MOD_RES         938
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         949
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         1..79
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042969"
FT   VAR_SEQ         219
FT                   /note="K -> KVLCPCLASQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042970"
FT   VAR_SEQ         556
FT                   /note="Q -> QA (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042971"
FT   VAR_SEQ         557
FT                   /note="A -> AG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_033861"
FT   VAR_SEQ         836
FT                   /note="T -> TS (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042972"
FT   VAR_SEQ         838..1165
FT                   /note="RGLPTDRYMWSDASGLQECTKAGTKPPSLQWAWVSDWFVDFSVPGGTDQEGW
FT                   QYASDFPASYHGSKTMKDFVRRRCWARKCKLVTSGPWLEVPPIALRDVSIIPESPGAEG
FT                   SGHSIALWAVSDKGDVLCRLGVSELNPAGSSWLHVGTDQPFASISIGACYQVWAVARDG
FT                   SAFYRGSVYPSQPAGDCWYHIPSPPRQRLKQVSAGQTSVYALDENGNLWYRQGITPSYP
FT                   QGSSWEHVSNNVCRVSVGPLDQVWVIANKVQGSHSLSRGTVCHRTGVQPHEPKGHGWDY
FT                   GIGGGWDHISVRANATRAPRSSSQEQEPSAPPEAHGPVCC -> SRDRISPCW (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042973"
FT   VARIANT         733
FT                   /note="S -> Y (in dbSNP:rs35623371)"
FT                   /id="VAR_060190"
FT   VARIANT         944
FT                   /note="P -> L (in dbSNP:rs11762014)"
FT                   /id="VAR_062238"
FT   CONFLICT        116
FT                   /note="W -> R (in Ref. 1; BAF85685)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="D -> Y (in Ref. 1; BAG51853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="A -> T (in Ref. 1; BAF85685)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        746
FT                   /note="S -> T (in Ref. 7; CAB55961)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        953
FT                   /note="I -> T (in Ref. 1; BAF85685)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        988
FT                   /note="P -> L (in Ref. 7; CAB55961)"
FT                   /evidence="ECO:0000305"
FT   HELIX           577..594
FT                   /evidence="ECO:0007829|PDB:4TQ1"
FT   TURN            595..599
FT                   /evidence="ECO:0007829|PDB:4TQ1"
FT   STRAND          600..603
FT                   /evidence="ECO:0007829|PDB:4TQ1"
SQ   SEQUENCE   1165 AA;  129696 MW;  D396F4128710062D CRC64;
     MPNSVLWAVD LFGRVYTLST AGQYWEMCKD SQLEFKRVSA TTQCCWGIAC DNQVYVYVCA
     SDVPIRRREE AYENQRWNPM GGFCEKLLLS DRWGWSDVSG LQHRPLDRVA LPSPHWEWES
     DWYVDENFGG EPTEKGGWTY AIDFPATYTK DKKWNSCVRR RKWIRYRRYK SRDIWAKIPS
     KDDPKELPDP FNDLSVGGWE ITEEPVGRLS VWAVSLQGKV WYREDVSHSN PEGSSWSLLD
     TPGEVVQISC GPHDLLWATL WEGQALVREG INRSNPKGSS WSIVEPPGSE NGVMHISVGV
     SVVWAVTKDW KVWFRRGVNS HNPCGTSWIE MVGEMTMVNV GMNDQVWGIG CEDRAVYFRQ
     GVTPSELSGK TWKAIIAARE CDRSHSGSSS SLLSAGCFFG DEVRGSGESA PSDTDASSEV
     ERPGPGQILP AEPLDDSKNA TGNSASGLGA GRTAEDTVED ACPAEGSREA RPNTHPGPAP
     TPAELPWTNI DLKEAKKVPS HSAAGFPETT SLSSLGLLPL GLEEPYGVDD HPLWAWVSGG
     GCVVEACAMP RWFTVQAGLS SSVHMLSLSI TPAQTAAWRK QIFQQLTERT KRELENFRHY
     EQAVEQSVWV KTGALQWWCD WKPHKWVDVR LALEQFTGHD GVRDSILFIY YVVHEEKKYI
     HIFLNEVVAL VPVLNETKHS FALYTPERTR QRWPVRLAAA TEQDMNDWLA LLSLSCCESR
     KVQGRPSPQA IWSITCKGDI FVSEPSPDLE AHEHPLPCDQ MFWRQMGGHL RMVEANSRGV
     VWGIGYDHTA WVYTGGYGGG CFQGLASSTS NIYTQSDVKC VHIYENQRWN PVTGYTSRGL
     PTDRYMWSDA SGLQECTKAG TKPPSLQWAW VSDWFVDFSV PGGTDQEGWQ YASDFPASYH
     GSKTMKDFVR RRCWARKCKL VTSGPWLEVP PIALRDVSII PESPGAEGSG HSIALWAVSD
     KGDVLCRLGV SELNPAGSSW LHVGTDQPFA SISIGACYQV WAVARDGSAF YRGSVYPSQP
     AGDCWYHIPS PPRQRLKQVS AGQTSVYALD ENGNLWYRQG ITPSYPQGSS WEHVSNNVCR
     VSVGPLDQVW VIANKVQGSH SLSRGTVCHR TGVQPHEPKG HGWDYGIGGG WDHISVRANA
     TRAPRSSSQE QEPSAPPEAH GPVCC
//