AEBP1_MOUSE
ID AEBP1_MOUSE Reviewed; 1128 AA.
AC Q640N1; O88442; Q3TVV5; Q3TWA7; Q3TX56; Q3TXB2; Q5NCI9; Q61281;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Adipocyte enhancer-binding protein 1;
DE Short=AE-binding protein 1;
DE AltName: Full=Aortic carboxypeptidase-like protein;
DE Flags: Precursor;
GN Name=Aebp1; Synonyms=Aclp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=7477299; DOI=10.1038/378092a0;
RA He G.-P., Muise A.M., Li A.W., Ro H.-S.;
RT "A eukaryotic transcriptional repressor with carboxypeptidase activity.";
RL Nature 378:92-96(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9624159; DOI=10.1074/jbc.273.25.15654;
RA Layne M.D., Endege W.O., Jain M.K., Yet S.-F., Hsieh C.-M., Chin M.T.,
RA Perrella M.A., Blanar M.A., Haber E., Lee M.-E.;
RT "Aortic carboxypeptidase-like protein, a novel protein with discoidin and
RT carboxypeptidase-like domains, is up-regulated during vascular smooth
RT muscle cell differentiation.";
RL J. Biol. Chem. 273:15654-15660(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=8920928; DOI=10.1006/bbrc.1996.1675;
RA Ohno I., Hashimoto J., Shimizu K., Takaoka K., Ochi T., Matsubara K.,
RA Okubo K.;
RT "A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its
RT expression in a differentiating osteoblastic cell line.";
RL Biochem. Biophys. Res. Commun. 228:411-414(1996).
RN [7]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH GNG5.
RX PubMed=10406805; DOI=10.1093/emboj/18.14.4004;
RA Park J.-G., Muise A.M., He G.-P., Kim S.-W., Ro H.-S.;
RT "Transcriptional regulation by the gamma5 subunit of a heterotrimeric G
RT protein during adipogenesis.";
RL EMBO J. 18:4004-4012(1999).
RN [8]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=11738825; DOI=10.1016/s0378-1119(01)00771-5;
RA Ro H.-S., Kim S.-W., Wu D., Webber C., Nicholson T.E.;
RT "Gene structure and expression of the mouse adipocyte enhancer-binding
RT protein.";
RL Gene 280:123-133(2001).
RN [9]
RP FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, AND DEVELOPMENTAL STAGE.
RX PubMed=11152475; DOI=10.1074/jbc.m010640200;
RA Kim S.-W., Muise A.M., Lyons P.J., Ro H.-S.;
RT "Regulation of adipogenesis by a transcriptional repressor that modulates
RT MAPK activation.";
RL J. Biol. Chem. 276:10199-10206(2001).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RX PubMed=11438679; DOI=10.1128/mcb.21.15.5256-5261.2001;
RA Layne M.D., Yet S.-F., Maemura K., Hsieh C.-M., Bernfield M.,
RA Perrella M.A., Lee M.-E.;
RT "Impaired abdominal wall development and deficient wound healing in mice
RT lacking aortic carboxypeptidase-like protein.";
RL Mol. Cell. Biol. 21:5256-5261(2001).
RN [11]
RP DEVELOPMENTAL STAGE.
RX PubMed=12072377; DOI=10.1210/endo.143.7.8875;
RA Gagnon A., Abaiian K.J., Crapper T., Layne M.D., Sorisky A.;
RT "Down-regulation of aortic carboxypeptidase-like protein during the early
RT phase of 3T3-L1 adipogenesis.";
RL Endocrinology 143:2478-2485(2002).
RN [12]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14729459; DOI=10.1016/j.yexcr.2003.10.020;
RA Abderrahim-Ferkoune A., Bezy O., Astri-Roques S., Elabd C., Ailhaud G.,
RA Amri E.-Z.;
RT "Transdifferentiation of preadipose cells into smooth muscle-like cells:
RT role of aortic carboxypeptidase-like protein.";
RL Exp. Cell Res. 293:219-228(2004).
RN [13]
RP DNA-BINDING, MUTAGENESIS OF THR-1003, AND PHOSPHORYLATION.
RX PubMed=15654748; DOI=10.1021/bi0480178;
RA Lyons P.J., Muise A.M., Ro H.-S.;
RT "MAPK modulates the DNA binding of adipocyte enhancer-binding protein 1.";
RL Biochemistry 44:926-931(2005).
RN [14]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15927179; DOI=10.1016/j.yexcr.2005.04.031;
RA Gagnon A., Landry A., Proulx J., Layne M.D., Sorisky A.;
RT "Aortic carboxypeptidase-like protein is regulated by transforming growth
RT factor beta in 3T3-L1 preadipocytes.";
RL Exp. Cell Res. 308:265-272(2005).
RN [15]
RP DEVELOPMENTAL STAGE.
RX PubMed=15749083; DOI=10.1016/j.modgep.2004.11.002;
RA Ith B., Wei J., Yet S.-F., Perrella M.A., Layne M.D.;
RT "Aortic carboxypeptidase-like protein is expressed in collagen-rich tissues
RT during mouse embryonic development.";
RL Gene Expr. Patterns 5:533-537(2005).
RN [16]
RP FUNCTION, AND INDUCTION.
RX PubMed=16307171; DOI=10.2119/2005-00021.ro;
RA Zhang L., Reidy S.P., Nicholson T.E., Lee H.-J., Majdalawieh A., Webber C.,
RA Stewart B.R., Dolphin P., Ro H.-S.;
RT "The role of AEBP1 in sex-specific diet-induced obesity.";
RL Mol. Med. 11:39-47(2005).
RN [17]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=16461908; DOI=10.1073/pnas.0508139103;
RA Majdalawieh A., Zhang L., Fuki I.V., Rader D.J., Ro H.-S.;
RT "Adipocyte enhancer-binding protein 1 is a potential novel atherogenic
RT factor involved in macrophage cholesterol homeostasis and inflammation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2346-2351(2006).
RN [18]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH CALMODULIN.
RX PubMed=16538615; DOI=10.1002/prot.20946;
RA Lyons P.J., Mattatall N.R., Ro H.-S.;
RT "Modeling and functional analysis of AEBP1, a transcriptional repressor.";
RL Proteins 63:1069-1083(2006).
RN [19]
RP FUNCTION, INTERACTION WITH NFKBIA, AND SUBCELLULAR LOCATION.
RX PubMed=17202411; DOI=10.1091/mbc.e06-03-0217;
RA Majdalawieh A., Zhang L., Ro H.-S.;
RT "Adipocyte enhancer-binding protein-1 promotes macrophage inflammatory
RT responsiveness by up-regulating NF-kappaB via IkappaBalpha negative
RT regulation.";
RL Mol. Biol. Cell 18:930-942(2007).
RN [20]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH PTEN.
RX PubMed=17299101; DOI=10.1038/oby.2007.569;
RA Ro H.-S., Zhang L., Majdalawieh A., Kim S.-W., Wu X., Lyons P.J.,
RA Webber C., Ma H., Reidy S.P., Boudreau A., Miller J.R., Mitchell P.,
RA McLeod R.S.;
RT "Adipocyte enhancer-binding protein 1 modulates adiposity and energy
RT homeostasis.";
RL Obesity 15:288-302(2007).
CC -!- FUNCTION: [Isoform 1]: As a positive regulator of collagen
CC fibrillogenesis, it is probably involved in the organization and
CC remodeling of the extracellular matrix. {ECO:0000250|UniProtKB:Q8IUX7}.
CC -!- FUNCTION: [Isoform 2]: May positively regulate MAP-kinase activity in
CC adipocytes, leading to enhanced adipocyte proliferation and reduced
CC adipocyte differentiation. May also positively regulate NF-kappa-B
CC activity in macrophages by promoting the phosphorylation and subsequent
CC degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage
CC inflammatory responsiveness. Can act as a transcriptional repressor.
CC {ECO:0000269|PubMed:10406805, ECO:0000269|PubMed:11152475,
CC ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:14729459,
CC ECO:0000269|PubMed:16307171, ECO:0000269|PubMed:16461908,
CC ECO:0000269|PubMed:16538615, ECO:0000269|PubMed:17202411,
CC ECO:0000269|PubMed:7477299}.
CC -!- SUBUNIT: Isoform 1: Interacts with different types of collagen,
CC including collagens I, III, and V (By similarity). Isoform 2: Interacts
CC with GNG5, NFKBIA, MAPK1, MAPK3 and PTEN. Interaction with MAPK1 may
CC stimulate DNA-binding. May interact with calmodulin. Binds to DNA in
CC vitro. {ECO:0000250|UniProtKB:Q8IUX7, ECO:0000269|PubMed:10406805,
CC ECO:0000269|PubMed:11152475, ECO:0000269|PubMed:16538615,
CC ECO:0000269|PubMed:17202411, ECO:0000269|PubMed:17299101}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:15927179}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:17202411, ECO:0000269|PubMed:9624159}. Nucleus
CC {ECO:0000269|PubMed:17202411}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Aclp;
CC IsoId=Q640N1-1; Sequence=Displayed;
CC Name=2; Synonyms=Aebp1;
CC IsoId=Q640N1-2; Sequence=VSP_033470;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in adipose
CC tissue, brain, heart, kidney, liver, lung, skeletal muscle, small
CC intestine, spleen and testis. Isoform 2 is expressed in macrophages.
CC Expressed in aorta, preadipocytes, adipocyte tissue, brain, heart,
CC liver, lung, skeletal muscle, skin and spleen (at protein level).
CC {ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:11738825,
CC ECO:0000269|PubMed:9624159}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the somites and dorsa from 9.5 dpc
CC and in the yolk sac and embryonic vasculature from 10.5 dpc. Expression
CC within the large and small blood vessels increases at 11.5 dpc and 13.5
CC dpc, with high expression in the vascular smooth muscle at 16.5 dpc.
CC Also expressed later in development in mesenchymal cells in the dermal
CC layer, the developing skeleton, connective tissue and the umbilical
CC ring and vessels. Up-regulated during vascular smooth muscle cell
CC differentiation and down-regulated during adipocyte differentiation and
CC osteoblast differentiation. {ECO:0000269|PubMed:11152475,
CC ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:12072377,
CC ECO:0000269|PubMed:14729459, ECO:0000269|PubMed:15749083,
CC ECO:0000269|PubMed:15927179, ECO:0000269|PubMed:7477299,
CC ECO:0000269|PubMed:8920928, ECO:0000269|PubMed:9624159}.
CC -!- INDUCTION: By TGF-beta. Expression is also induced by a high fat diet.
CC {ECO:0000269|PubMed:15927179, ECO:0000269|PubMed:16307171}.
CC -!- DOMAIN: [Isoform 1]: The F5/8 type C domain binds to different types of
CC collagen, including collagens I, III, and V.
CC {ECO:0000250|UniProtKB:Q8IUX7}.
CC -!- PTM: Phosphorylated by MAPK1 in vitro. {ECO:0000269|PubMed:15654748}.
CC -!- DISRUPTION PHENOTYPE: Two independent knockout mice have been generated
CC for the gene encoding this protein, and these exhibit different
CC phenotypes. Mice lacking exons 7-12 exhibit reduced growth rate and
CC body weight and resistance to dietary-induced obesity. Individual
CC adipocytes from these animals are hypoproliferative while the adipose
CC tissue is prone to apoptosis. Mice lacking exons 7-16 die perinatally
CC from gastroschisis, in which abdominal viscera are extruded through the
CC ventral body wall. Surviving mice exhibit deficient wound healing,
CC having dermal fibroblasts with reduced proliferative capacity. Mice
CC lacking exons 7-16 may exhibit phenotypes arising from effects on the
CC locus encoding Pold2, which lies immediately downstream of this locus.
CC {ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:17299101}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- CAUTION: Although related to peptidase M14 family, lacks the active
CC site residues and zinc-binding sites, suggesting that it has no
CC carboxypeptidase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56648.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X80478; CAA56648.1; ALT_FRAME; mRNA.
DR EMBL; AF053943; AAC25584.1; -; mRNA.
DR EMBL; AK159330; BAE34995.1; -; mRNA.
DR EMBL; AK159342; BAE35004.1; -; mRNA.
DR EMBL; AK159377; BAE35033.1; -; mRNA.
DR EMBL; AK159409; BAE35060.1; -; mRNA.
DR EMBL; AK159774; BAE35359.1; -; mRNA.
DR EMBL; AK159957; BAE35513.1; -; mRNA.
DR EMBL; AL627069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082577; AAH82577.1; -; mRNA.
DR CCDS; CCDS24406.1; -. [Q640N1-1]
DR PIR; S60227; S51739.
DR RefSeq; NP_001278786.1; NM_001291857.2.
DR RefSeq; NP_033766.2; NM_009636.3. [Q640N1-1]
DR AlphaFoldDB; Q640N1; -.
DR SMR; Q640N1; -.
DR BioGRID; 198013; 5.
DR IntAct; Q640N1; 2.
DR STRING; 10090.ENSMUSP00000099987; -.
DR MEROPS; M14.951; -.
DR GlyGen; Q640N1; 1 site.
DR iPTMnet; Q640N1; -.
DR PhosphoSitePlus; Q640N1; -.
DR CPTAC; non-CPTAC-3446; -.
DR MaxQB; Q640N1; -.
DR PaxDb; Q640N1; -.
DR PeptideAtlas; Q640N1; -.
DR PRIDE; Q640N1; -.
DR ProteomicsDB; 281942; -. [Q640N1-1]
DR ProteomicsDB; 281943; -. [Q640N1-2]
DR Antibodypedia; 4099; 198 antibodies from 29 providers.
DR DNASU; 11568; -.
DR Ensembl; ENSMUST00000102923; ENSMUSP00000099987; ENSMUSG00000020473. [Q640N1-1]
DR Ensembl; ENSMUST00000109829; ENSMUSP00000105454; ENSMUSG00000020473. [Q640N1-2]
DR GeneID; 11568; -.
DR KEGG; mmu:11568; -.
DR UCSC; uc007hxg.3; mouse. [Q640N1-1]
DR CTD; 165; -.
DR MGI; MGI:1197012; Aebp1.
DR VEuPathDB; HostDB:ENSMUSG00000020473; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158323; -.
DR HOGENOM; CLU_006722_0_1_1; -.
DR InParanoid; Q640N1; -.
DR OMA; PHYDDMD; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q640N1; -.
DR TreeFam; TF315592; -.
DR BioGRID-ORCS; 11568; 0 hits in 60 CRISPR screens.
DR ChiTaRS; Aebp1; mouse.
DR PRO; PR:Q640N1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q640N1; protein.
DR Bgee; ENSMUSG00000020473; Expressed in ascending aorta and 243 other tissues.
DR Genevisible; Q640N1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:MGI.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1904026; P:regulation of collagen fibril organization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR CDD; cd00057; FA58C; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cytoplasm; DNA-binding;
KW Glycoprotein; Nucleus; Reference proteome; Repressor; Secreted; Signal;
KW Transcription; Transcription regulation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1128
FT /note="Adipocyte enhancer-binding protein 1"
FT /id="PRO_0000333190"
FT DOMAIN 374..531
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 40..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..546
FT /note="Required for DNA-binding and interaction with
FT NFKBIA"
FT /evidence="ECO:0000269|PubMed:17202411"
FT REGION 412..615
FT /note="Interaction with MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:11152475"
FT REGION 546..976
FT /note="Interaction with PTEN"
FT /evidence="ECO:0000269|PubMed:17299101"
FT REGION 932..1128
FT /note="Required for transcriptional repression"
FT REGION 997..1128
FT /note="Interaction with MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:11152475"
FT COMPBIAS 69..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..380
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7477299"
FT /id="VSP_033470"
FT MUTAGEN 1003
FT /note="T->A: Impairs DNA-binding and phosphorylation by
FT MAPK1."
FT /evidence="ECO:0000269|PubMed:15654748"
FT MUTAGEN 1003
FT /note="T->D: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:15654748"
FT CONFLICT 333
FT /note="K -> E (in Ref. 3; BAE34995/BAE35004)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="K -> KA (in Ref. 3; BAE35359/BAE35513/BAE34995/
FT BAE35004/BAE35033/BAE35060)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="S -> F (in Ref. 3; BAE35359/BAE35513)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="S -> C (in Ref. 3; BAE35359)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="R -> G (in Ref. 2; AAC25584)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="I -> IEE (in Ref. 3; BAE35359/BAE35513/BAE34995/
FT BAE35004/BAE35033/BAE35060)"
FT /evidence="ECO:0000305"
FT CONFLICT 1115
FT /note="L -> F (in Ref. 3; BAE35359/BAE35513/BAE34995/
FT BAE35004/BAE35033/BAE35060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1128 AA; 128365 MW; C24F46B893C02DC9 CRC64;
MAPVRTASLL CGLLALLTLC PEGNPQTVLT DDEIEEFLEG FLSELETQSP PREDDVEVQP
LPEPTQRPRK SKAGGKQRAD VEVPPEKNKD KEKKGKKDKG PKATKPLEGS TRPTKKPKEK
PPKATKKPKE KPPKATKKPK EKPPKATKKP KEKPPKATKR PSAGKKFSTV APLETLDRLL
PSPSNPSAQE LPQKRDTPFP NAWQGQGEET QVEAKQPRPE PEEETEMPTL DYNDQIEKED
YEDFEYIRRQ KQPRPTPSRR RLWPERPEEK TEEPEERKEV EPPLKPLLPP DYGDSYVIPN
YDDLDYYFPH PPPQKPDVGQ EVDEEKEEMK KPKKEGSSPK EDTEDKWTVE KNKDHKGPRK
GEELEEEWAP VEKIKCPPIG MESHRIEDNQ IRASSMLRHG LGAQRGRLNM QAGANEDDYY
DGAWCAEDES QTQWIEVDTR RTTRFTGVIT QGRDSSIHDD FVTTFFVGFS NDSQTWVMYT
NGYEEMTFYG NVDKDTPVLS ELPEPVVARF IRIYPLTWNG SLCMRLEVLG CPVTPVYSYY
AQNEVVTTDS LDFRHHSYKD MRQLMKAVNE ECPTITRTYS LGKSSRGLKI YAMEISDNPG
DHELGEPEFR YTAGIHGNEV LGRELLLLLM QYLCQEYRDG NPRVRNLVQD TRIHLVPSLN
PDGYEVAAQM GSEFGNWALG LWTEEGFDIF EDFPDLNSVL WAAEEKKWVP YRVPNNNLPI
PERYLSPDAT VSTEVRAIIS WMEKNPFVLG ANLNGGERLV SYPYDMARTP SQEQLLAEAL
AAARGEDDDG VSEAQETPDH AIFRWLAISF ASAHLTMTEP YRGGCQAQDY TSGMGIVNGA
KWNPRSGTFN DFSYLHTNCL ELSVYLGCDK FPHESELPRE WENNKEALLT FMEQVHRGIK
GVVTDEQGIP IANATISVSG INHGVKTASG GDYWRILNPG EYRVTAHAEG YTSSAKICNV
DYDIGATQCN FILARSNWKR IREILAMNGN RPILRVDPSR PMTPQQRRMQ QRRLQYRLRM
REQMRLRRLN STAGPATSPT PALMPPPSPT PAITLRPWEV LPTTTAGWEE SETETYTEVV
TEFETEYGTD LEVEEIEEEE EEEEEEMDTG LTFPLTTVET YTVNFGDF
