BACD3_HUMAN
ID BACD3_HUMAN Reviewed; 313 AA.
AC Q9H3F6; Q53HN2; Q59FV1; Q6PL47; Q96SU0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3 {ECO:0000303|PubMed:19782033};
DE Short=hBACURD3 {ECO:0000303|PubMed:19782033};
DE AltName: Full=BTB/POZ domain-containing protein KCTD10;
DE AltName: Full=Potassium channel tetramerization domain-containing protein 10;
GN Name=KCTD10; Synonyms=ULR061; ORFNames=MSTP028;
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).
RC TISSUE=Uterine leiomyoma;
RA Li B., Hu Z.-H., Yang J., Zhang Y.-L.;
RT "Identification and characterization of a human uterine leiomyoma related
RT gene through bioinformatics.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Li H., Zhong G., Ke R., Shen C., Zhou G., Lin L., Yang S.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP 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 SUBCELLULAR LOCATION, AND INTERACTION WITH PCNA.
RX PubMed=19125419; DOI=10.1002/jcb.22026;
RA Wang Y., Zheng Y., Luo F., Fan X., Chen J., Zhang C., Hui R.;
RT "KCTD10 interacts with proliferating cell nuclear antigen and its down-
RT regulation could inhibit cell proliferation.";
RL J. Cell. Biochem. 106:409-413(2009).
RN [11]
RP IDENTIFICATION.
RX PubMed=19782033; DOI=10.1016/j.molcel.2009.09.004;
RA Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M.,
RA Peng H.B., Shao F.;
RT "Cullin mediates degradation of RhoA through evolutionarily conserved BTB
RT adaptors to control actin cytoskeleton structure and cell movement.";
RL Mol. Cell 35:841-855(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 26-135, AND SUBUNIT.
RX PubMed=28963344; DOI=10.1042/bcj20170527;
RA Pinkas D.M., Sanvitale C.E., Bufton J.C., Sorrell F.J., Solcan N.,
RA Chalk R., Doutch J., Bullock A.N.;
RT "Structural complexity in the KCTD family of Cullin3-dependent E3 ubiquitin
RT ligases.";
RL Biochem. J. 474:3747-3761(2017).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase
CC complex mediates the ubiquitination of target proteins, leading to
CC their degradation by the proteasome (By similarity).
CC {ECO:0000250|UniProtKB:Q8WZ19}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homotetramer; forms a two-fold symmetric tetramer in solution
CC (PubMed:28963344). Interacts with CUL3; interaction is direct and forms
CC a 5:5 heterodecamer (PubMed:28963344). Component of the BCR(BACURD3) E3
CC ubiquitin ligase complex, at least composed of CUL3, KCTD10/BACURD3 and
CC RBX1 (By similarity). Interacts with DNA polymerase delta subunit
CC 2/POLD2 (By similarity). Interacts with PCNA (PubMed:19125419).
CC {ECO:0000250|UniProtKB:Q7TPL3, ECO:0000250|UniProtKB:Q8WZ19,
CC ECO:0000269|PubMed:19125419, ECO:0000269|PubMed:28963344}.
CC -!- INTERACTION:
CC Q9H3F6; Q13618: CUL3; NbExp=6; IntAct=EBI-2505886, EBI-456129;
CC Q9H3F6; Q92997: DVL3; NbExp=3; IntAct=EBI-2505886, EBI-739789;
CC Q9H3F6; Q9H3F6: KCTD10; NbExp=3; IntAct=EBI-2505886, EBI-2505886;
CC Q9H3F6; Q8WZ19: KCTD13; NbExp=4; IntAct=EBI-2505886, EBI-742916;
CC Q9H3F6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2505886, EBI-741158;
CC Q9H3F6; Q15560: TCEA2; NbExp=3; IntAct=EBI-2505886, EBI-710310;
CC Q9H3F6; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-2505886, EBI-11523345;
CC Q9H3F6; Q13829: TNFAIP1; NbExp=6; IntAct=EBI-2505886, EBI-2505861;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19125419}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H3F6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3F6-2; Sequence=VSP_019980;
CC Name=3;
CC IsoId=Q9H3F6-3; Sequence=VSP_019978, VSP_019979;
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55188.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD92595.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY205299; AAO47716.1; -; mRNA.
DR EMBL; AF113208; AAG39279.1; -; mRNA.
DR EMBL; AY597809; AAT09002.1; -; mRNA.
DR EMBL; AK027543; BAB55188.1; ALT_INIT; mRNA.
DR EMBL; AB209358; BAD92595.1; ALT_INIT; mRNA.
DR EMBL; AK222548; BAD96268.1; -; mRNA.
DR EMBL; AC007570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040062; AAH40062.1; -; mRNA.
DR CCDS; CCDS9128.1; -. [Q9H3F6-1]
DR RefSeq; NP_001304324.1; NM_001317395.1.
DR RefSeq; NP_001304328.1; NM_001317399.1. [Q9H3F6-2]
DR RefSeq; NP_114160.1; NM_031954.4. [Q9H3F6-1]
DR PDB; 5FTA; X-ray; 2.64 A; A/B/C/D=26-135.
DR PDBsum; 5FTA; -.
DR AlphaFoldDB; Q9H3F6; -.
DR SMR; Q9H3F6; -.
DR BioGRID; 123803; 210.
DR IntAct; Q9H3F6; 51.
DR STRING; 9606.ENSP00000228495; -.
DR iPTMnet; Q9H3F6; -.
DR PhosphoSitePlus; Q9H3F6; -.
DR BioMuta; KCTD10; -.
DR DMDM; 74733570; -.
DR EPD; Q9H3F6; -.
DR jPOST; Q9H3F6; -.
DR MassIVE; Q9H3F6; -.
DR MaxQB; Q9H3F6; -.
DR PaxDb; Q9H3F6; -.
DR PeptideAtlas; Q9H3F6; -.
DR PRIDE; Q9H3F6; -.
DR ProteomicsDB; 80705; -. [Q9H3F6-1]
DR ProteomicsDB; 80706; -. [Q9H3F6-2]
DR ProteomicsDB; 80707; -. [Q9H3F6-3]
DR Antibodypedia; 2841; 125 antibodies from 19 providers.
DR DNASU; 83892; -.
DR Ensembl; ENST00000228495.11; ENSP00000228495.6; ENSG00000110906.13. [Q9H3F6-1]
DR GeneID; 83892; -.
DR KEGG; hsa:83892; -.
DR MANE-Select; ENST00000228495.11; ENSP00000228495.6; NM_031954.5; NP_114160.1.
DR UCSC; uc001toi.2; human. [Q9H3F6-1]
DR CTD; 83892; -.
DR DisGeNET; 83892; -.
DR GeneCards; KCTD10; -.
DR HGNC; HGNC:23236; KCTD10.
DR HPA; ENSG00000110906; Low tissue specificity.
DR MIM; 613421; gene.
DR neXtProt; NX_Q9H3F6; -.
DR OpenTargets; ENSG00000110906; -.
DR PharmGKB; PA134938409; -.
DR VEuPathDB; HostDB:ENSG00000110906; -.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR HOGENOM; CLU_060008_0_0_1; -.
DR InParanoid; Q9H3F6; -.
DR OMA; IKYPSEY; -.
DR OrthoDB; 804210at2759; -.
DR PhylomeDB; Q9H3F6; -.
DR TreeFam; TF315649; -.
DR PathwayCommons; Q9H3F6; -.
DR SignaLink; Q9H3F6; -.
DR SIGNOR; Q9H3F6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 83892; 262 hits in 1133 CRISPR screens.
DR ChiTaRS; KCTD10; human.
DR GenomeRNAi; 83892; -.
DR Pharos; Q9H3F6; Tbio.
DR PRO; PR:Q9H3F6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H3F6; protein.
DR Bgee; ENSG00000110906; Expressed in epithelial cell of pancreas and 180 other tissues.
DR ExpressionAtlas; Q9H3F6; baseline and differential.
DR Genevisible; Q9H3F6; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005112; F:Notch binding; IPI:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045068; BACURD1-3.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR PANTHER; PTHR11145; PTHR11145; 1.
DR Pfam; PF02214; BTB_2; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..313
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 3"
FT /id="PRO_0000247421"
FT DOMAIN 32..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT MOTIF 239..245
FT /note="PCNA-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..158
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_019978"
FT VAR_SEQ 159..175
FT /note="PAVKLLYNRSNNKYSYT -> MMAVFTSLWSPYQMLFC (in isoform
FT 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_019979"
FT VAR_SEQ 176..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019980"
FT CONFLICT 1
FT /note="M -> V (in Ref. 4; BAB55188)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> P (in Ref. 3; AAT09002)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="N -> T (in Ref. 6; BAD96268)"
FT /evidence="ECO:0000305"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:5FTA"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:5FTA"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5FTA"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:5FTA"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:5FTA"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5FTA"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:5FTA"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:5FTA"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:5FTA"
SQ SEQUENCE 313 AA; 35432 MW; 199AF07A30D5BCA6 CRC64;
MEEMSGESVV SSAVPAAATR TTSFKGTSPS SKYVKLNVGG ALYYTTMQTL TKQDTMLKAM
FSGRMEVLTD SEGWILIDRC GKHFGTILNY LRDGAVPLPE SRREIEELLA EAKYYLVQGL
VEECQAALQN KDTYEPFCKV PVITSSKEEQ KLIATSNKPA VKLLYNRSNN KYSYTSNSDD
NMLKNIELFD KLSLRFNGRV LFIKDVIGDE ICCWSFYGQG RKIAEVCCTS IVYATEKKQT
KVEFPEARIY EETLNILLYE AQDGRGPDNA LLEATGGAAG RSHHLDEDEE RERIERVRRI
HIKRPDDRAH LHQ
