TCPR1_HUMAN
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 03-AUG-2022, entry version 150.
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 Q7Z6L1; Q9H492: MAP1LC3A; NbExp=2; IntAct=EBI-2946676, EBI-720768;
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 PDBsum; 4TQ1; -.
DR AlphaFoldDB; Q7Z6L1; -.
DR SMR; Q7Z6L1; -.
DR BioGRID; 117375; 12.
DR ComplexPortal; CPX-358; ATG5-ATG12-TECPR1 complex.
DR IntAct; Q7Z6L1; 16.
DR STRING; 9606.ENSP00000404923; -.
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; Q7Z6L1; -.
DR PeptideAtlas; Q7Z6L1; -.
DR PRIDE; Q7Z6L1; -.
DR ProteomicsDB; 69439; -. [Q7Z6L1-1]
DR ProteomicsDB; 69440; -. [Q7Z6L1-2]
DR ProteomicsDB; 69441; -. [Q7Z6L1-3]
DR ProteomicsDB; 69442; -. [Q7Z6L1-4]
DR Antibodypedia; 8742; 126 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 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; 119234at2759; -.
DR PhylomeDB; Q7Z6L1; -.
DR TreeFam; TF323648; -.
DR PathwayCommons; Q7Z6L1; -.
DR SignaLink; Q7Z6L1; -.
DR BioGRID-ORCS; 25851; 11 hits in 1076 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 179 other tissues.
DR ExpressionAtlas; Q7Z6L1; baseline and differential.
DR Genevisible; Q7Z6L1; HS.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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; IC: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 Gene3D; 2.30.29.30; -; 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 Pfam; PF06462; Hyd_WA; 2.
DR Pfam; PF06398; Pex24p; 2.
DR Pfam; PF19193; Tectonin; 2.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM00706; TECPR; 11.
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
