GenomeNet

Database: UniProt
Entry: O88712
LinkDB: O88712
Original site: O88712 
ID   CTBP1_MOUSE             Reviewed;         441 AA.
AC   O88712; Q3TAT1; Q3TDL5; Q3TUM5; Q91WI6; Q91YX3; Q9QYG2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   13-FEB-2019, entry version 174.
DE   RecName: Full=C-terminal-binding protein 1;
DE            Short=CtBP1;
DE            EC=1.1.1.-;
GN   Name=Ctbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=10369679; DOI=10.1093/emboj/18.12.3392;
RA   Criqui-Filipe P., Ducret C., Maira S.-M., Wasylyk B.;
RT   "Net, a negative Ras-switchable TCF, contains a second inhibition
RT   domain, the CID, that mediates repression through interactions with
RT   CtBP and de-acetylation.";
RL   EMBO J. 18:3392-3403(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=ICR;
RX   PubMed=10567582; DOI=10.1128/MCB.19.12.8581;
RA   Furusawa T., Moribe H., Kondoh H., Higashi Y.;
RT   "Identification of CtBP1 and CtBP2 as corepressors of zinc finger-
RT   homeodomain factor deltaEF1.";
RL   Mol. Cell. Biol. 19:8581-8590(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=129, FVB/N, and FVB/N-3;
RC   TISSUE=Mammary tumor, and Salivary gland;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 98-108 AND 286-305, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH HDAC4; HDAC5 AND HDAC9.
RX   PubMed=11022042; DOI=10.1074/jbc.M007364200;
RA   Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
RT   "Association of COOH-terminal-binding protein (CtBP) and MEF2-
RT   interacting transcription repressor (MITR) contributes to
RT   transcriptional repression of the MEF2 transcription factor.";
RL   J. Biol. Chem. 276:35-39(2001).
RN   [7]
RP   INTERACTION WITH HIPK2.
RX   PubMed=14567915; DOI=10.1016/S0092-8674(03)00802-X;
RA   Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.;
RT   "Homeodomain interacting protein kinase 2 promotes apoptosis by
RT   downregulating the transcriptional corepressor CtBP.";
RL   Cell 115:177-186(2003).
RN   [8]
RP   INTERACTION WITH NRIP1.
RX   PubMed=14736873; DOI=10.1074/jbc.M313906200;
RA   Christian M., Tullet J.M.A., Parker M.G.;
RT   "Characterization of four autonomous repression domains in the
RT   corepressor receptor interacting protein 140.";
RL   J. Biol. Chem. 279:15645-15651(2004).
RN   [9]
RP   INTERACTION WITH FOXP1 AND FOXP2.
RX   PubMed=14701752; DOI=10.1128/MCB.24.2.809-822.2004;
RA   Li S., Weidenfeld J., Morrisey E.E.;
RT   "Transcriptional and DNA binding activity of the Foxp1/2/4 family is
RT   modulated by heterotypic and homotypic protein interactions.";
RL   Mol. Cell. Biol. 24:809-822(2004).
RN   [10]
RP   INTERACTION WITH GLIS2, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16326862; DOI=10.1093/nar/gki985;
RA   Kim S.-C., Kim Y.-S., Jetten A.M.;
RT   "Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses
RT   transcription through interaction with C-terminal binding protein 1
RT   (CtBP1).";
RL   Nucleic Acids Res. 33:6805-6815(2005).
RN   [11]
RP   INTERACTION WITH WIZ.
RX   PubMed=16702210; DOI=10.1074/jbc.M603087200;
RA   Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT   "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to
RT   the co-repressor molecule CtBP.";
RL   J. Biol. Chem. 281:20120-20128(2006).
RN   [12]
RP   FUNCTION, INTERACTION WITH PRDM16, AND SUBCELLULAR LOCATION.
RX   PubMed=18483224; DOI=10.1101/gad.1666108;
RA   Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
RA   Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
RT   "Regulation of the brown and white fat gene programs through a
RT   PRDM16/CtBP transcriptional complex.";
RL   Genes Dev. 22:1397-1409(2008).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH SATB1.
RX   PubMed=19103759; DOI=10.1128/MCB.00822-08;
RA   Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.;
RT   "Acetylation-dependent interaction of SATB1 and CtBP1 mediates
RT   transcriptional repression by SATB1.";
RL   Mol. Cell. Biol. 29:1321-1337(2009).
RN   [14]
RP   INTERACTION WITH IKZF4.
RX   PubMed=19696312; DOI=10.1126/science.1176077;
RA   Pan F., Yu H., Dang E.V., Barbi J., Pan X., Grosso J.F., Jinasena D.,
RA   Sharma S.M., McCadden E.M., Getnet D., Drake C.G., Liu J.O.,
RA   Ostrowski M.C., Pardoll D.M.;
RT   "Eos mediates Foxp3-dependent gene silencing in CD4+ regulatory T
RT   cells.";
RL   Science 325:1142-1146(2009).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Corepressor targeting diverse transcription regulators
CC       such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in
CC       controlling the equilibrium between tubular and stacked structures
CC       in the Golgi complex. Functions in brown adipose tissue (BAT)
CC       differentiation. {ECO:0000269|PubMed:10369679,
CC       ECO:0000269|PubMed:10567582, ECO:0000269|PubMed:16326862,
CC       ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:19103759}.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Note=Cofactor binding induces a conformational change.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts
CC       with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its
CC       PXDLS motif). Interacts with PNN, MECOM and ZFHX1B. Interacts with
CC       ZNF366 (via PXDLS motif) (By similarity). Interaction with SATB1
CC       (non-acetylated form); the interaction stabilizes its attachment
CC       to DNA and promotes transcription repression. Interacts with
CC       PRDM16; the interaction represses white adipose tissue (WAT)-
CC       specific genes expression. Interacts with GLIS2, HIPK2, FOXP1,
CC       FOXP2, HDAC4, HDAC5, HDAC9, NRIP1, WIZ and ZNF217. Interacts with
CC       BCL6; the interaction is required for BCL6 transcriptional
CC       autoinhibition and inhibition of some BCL6 target genes. Interacts
CC       with IKZF4. Interacts with MCRIP1 (unphosphorylated form, via the
CC       PXDLS motif); competitively inhibiting CTBP-ZEB1 interaction (By
CC       similarity). {ECO:0000250|UniProtKB:Q13363,
CC       ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:14567915,
CC       ECO:0000269|PubMed:14701752, ECO:0000269|PubMed:14736873,
CC       ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:16702210,
CC       ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:19103759,
CC       ECO:0000269|PubMed:19696312}.
CC   -!- INTERACTION:
CC       Q14526:HIC1 (xeno); NbExp=10; IntAct=EBI-604547, EBI-2507362;
CC       Q64318:Zeb1; NbExp=5; IntAct=EBI-604547, EBI-8560245;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13363}.
CC       Nucleus {ECO:0000250|UniProtKB:Q13363}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O88712-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88712-2; Sequence=VSP_024738;
CC       Name=3;
CC         IsoId=O88712-3; Sequence=VSP_024737;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in a wide range of adult tissues.
CC       {ECO:0000269|PubMed:10567582}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the developmental
CC       stages. {ECO:0000269|PubMed:10567582}.
CC   -!- PTM: ADP-ribosylated; when cells are exposed to brefeldin A.
CC       {ECO:0000250}.
CC   -!- PTM: The level of phosphorylation appears to be regulated during
CC       the cell cycle. Phosphorylation by HIPK2 on Ser-423 induces
CC       proteasomal degradation (By similarity). {ECO:0000250}.
CC   -!- PTM: Sumoylation on Lys-429 is promoted by the E3 SUMO-protein
CC       ligase CBX4. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE41586.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AJ010483; CAA09219.1; -; mRNA.
DR   EMBL; AB033122; BAA85180.1; -; mRNA.
DR   EMBL; AK133816; BAE21859.1; -; mRNA.
DR   EMBL; AK160658; BAE35946.1; -; mRNA.
DR   EMBL; AK165276; BAE38115.1; -; mRNA.
DR   EMBL; AK170133; BAE41586.1; ALT_INIT; mRNA.
DR   EMBL; AK171650; BAE42587.1; -; mRNA.
DR   EMBL; BC013702; AAH13702.1; -; mRNA.
DR   EMBL; BC015071; AAH15071.1; -; mRNA.
DR   EMBL; BC042425; AAH42425.1; -; mRNA.
DR   CCDS; CCDS19201.1; -. [O88712-1]
DR   CCDS; CCDS80255.1; -. [O88712-3]
DR   RefSeq; NP_001185788.1; NM_001198859.1.
DR   RefSeq; NP_001185789.1; NM_001198860.1.
DR   RefSeq; NP_001185790.1; NM_001198861.1. [O88712-2]
DR   RefSeq; NP_001297464.1; NM_001310535.1. [O88712-3]
DR   RefSeq; NP_038530.1; NM_013502.3. [O88712-1]
DR   UniGene; Mm.240076; -.
DR   UniGene; Mm.7286; -.
DR   ProteinModelPortal; O88712; -.
DR   SMR; O88712; -.
DR   BioGrid; 198961; 18.
DR   CORUM; O88712; -.
DR   DIP; DIP-33907N; -.
DR   IntAct; O88712; 20.
DR   MINT; O88712; -.
DR   STRING; 10090.ENSMUSP00000078682; -.
DR   iPTMnet; O88712; -.
DR   PhosphoSitePlus; O88712; -.
DR   MaxQB; O88712; -.
DR   PaxDb; O88712; -.
DR   PeptideAtlas; O88712; -.
DR   PRIDE; O88712; -.
DR   Ensembl; ENSMUST00000079746; ENSMUSP00000078682; ENSMUSG00000037373. [O88712-1]
DR   Ensembl; ENSMUST00000201575; ENSMUSP00000144554; ENSMUSG00000037373. [O88712-3]
DR   GeneID; 13016; -.
DR   KEGG; mmu:13016; -.
DR   UCSC; uc008xaj.2; mouse. [O88712-1]
DR   UCSC; uc008xak.2; mouse. [O88712-2]
DR   CTD; 1487; -.
DR   MGI; MGI:1201685; Ctbp1.
DR   eggNOG; KOG0067; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   GeneTree; ENSGT00940000157061; -.
DR   HOVERGEN; HBG001898; -.
DR   InParanoid; O88712; -.
DR   KO; K04496; -.
DR   OMA; YHAIGIR; -.
DR   OrthoDB; 700058at2759; -.
DR   PhylomeDB; O88712; -.
DR   TreeFam; TF313593; -.
DR   Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-MMU-4641265; Repression of WNT target genes.
DR   ChiTaRS; Ctbp1; mouse.
DR   PRO; PR:O88712; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000037373; Expressed in 302 organ(s), highest expression level in ear.
DR   ExpressionAtlas; O88712; baseline and differential.
DR   Genevisible; O88712; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; ISO:MGI.
DR   GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0006342; P:chromatin silencing; ISO:MGI.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; ISO:MGI.
DR   GO; GO:0090241; P:negative regulation of histone H4 acetylation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR   GO; GO:0099526; P:presynapse to nucleus signaling pathway; ISO:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR   GO; GO:0050872; P:white fat cell differentiation; IDA:UniProtKB.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   ADP-ribosylation; Alternative splicing; Complete proteome; Cytoplasm;
KW   Differentiation; Direct protein sequencing; Isopeptide bond; NAD;
KW   Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    441       C-terminal-binding protein 1.
FT                                /FTId=PRO_0000076042.
FT   NP_BIND     180    185       NAD. {ECO:0000250}.
FT   NP_BIND     237    243       NAD. {ECO:0000250}.
FT   NP_BIND     264    266       NAD. {ECO:0000250}.
FT   NP_BIND     315    318       NAD. {ECO:0000250}.
FT   REGION        1     70       Interaction with GLIS2 1.
FT   REGION      288    360       Interaction with GLIS2 2.
FT   ACT_SITE    266    266       {ECO:0000250}.
FT   ACT_SITE    295    295       {ECO:0000250}.
FT   ACT_SITE    315    315       Proton donor. {ECO:0000250}.
FT   BINDING     100    100       NAD. {ECO:0000250}.
FT   BINDING     204    204       NAD. {ECO:0000250}.
FT   BINDING     290    290       NAD. {ECO:0000250}.
FT   MOD_RES     300    300       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13363}.
FT   MOD_RES     423    423       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13363}.
FT   CROSSLNK    429    429       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ       1     74       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024737.
FT   VAR_SEQ       1     13       MGSSHLLNKGLPL -> MS (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024738.
FT   CONFLICT     55     55       D -> G (in Ref. 3; BAE41586/BAE42587).
FT                                {ECO:0000305}.
FT   CONFLICT    108    108       K -> R (in Ref. 3; BAE35946).
FT                                {ECO:0000305}.
FT   CONFLICT    380    380       Missing (in Ref. 1; CAA09219 and 3;
FT                                BAE35946). {ECO:0000305}.
SQ   SEQUENCE   441 AA;  47745 MW;  2105CC8D69D915F4 CRC64;
     MGSSHLLNKG LPLGVRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
     EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV
     PAASVEETAD STLCHILNLY RRTTWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII
     GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN
     EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
     QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT
     HWASMDPAVV HPELNGAAYS RYPPGVVSVA PTGIPAAVEG IVPSAMSLSH GLPPVAHPPH
     APSPGQTVKP EADRDHTSDQ L
//
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