AEBP1_RAT
ID AEBP1_RAT Reviewed; 1128 AA.
AC A2RUV9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP TISSUE 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 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).
CC -!- FUNCTION: As a positive regulator of collagen fibrillogenesis, it is
CC probably involved in the organization and remodeling of the
CC extracellular matrix (By similarity). May positively regulate MAP-
CC kinase activity in adipocytes, leading to enhanced adipocyte
CC proliferation and reduced adipocyte differentiation. May also
CC positively regulate NF-kappa-B activity in macrophages by promoting the
CC phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA),
CC leading to enhanced macrophage inflammatory responsiveness. Can act as
CC a transcriptional repressor. {ECO:0000250|UniProtKB:Q640N1,
CC ECO:0000250|UniProtKB:Q8IUX7}.
CC -!- SUBUNIT: Interacts with different types of collagen, including
CC collagens I, III, and V (By similarity). Interacts with GNG5, NFKBIA,
CC MAPK1, MAPK3 and PTEN. May interact with calmodulin. Interaction with
CC MAPK1 may stimulate DNA-binding. Binds to DNA in vitro.
CC {ECO:0000250|UniProtKB:Q640N1, ECO:0000250|UniProtKB:Q8IUX7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q640N1}.
CC -!- TISSUE SPECIFICITY: Expressed in aorta. {ECO:0000269|PubMed:11738825,
CC ECO:0000269|PubMed:9624159}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in quiescent cells.
CC {ECO:0000269|PubMed:9624159}.
CC -!- DOMAIN: The F5/8 type C domain binds to different types of collagen,
CC including collagens I, III, and V. {ECO:0000250|UniProtKB:Q8IUX7}.
CC -!- PTM: Phosphorylated by MAPK1 in vitro. {ECO:0000250}.
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}.
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DR EMBL; BC133065; AAI33066.1; -; mRNA.
DR RefSeq; NP_001094440.1; NM_001100970.1.
DR AlphaFoldDB; A2RUV9; -.
DR SMR; A2RUV9; -.
DR STRING; 10116.ENSRNOP00000018846; -.
DR MEROPS; M14.951; -.
DR GlyGen; A2RUV9; 1 site.
DR PaxDb; A2RUV9; -.
DR PRIDE; A2RUV9; -.
DR Ensembl; ENSRNOT00000018846; ENSRNOP00000018846; ENSRNOG00000013720.
DR GeneID; 305494; -.
DR KEGG; rno:305494; -.
DR UCSC; RGD:1306922; rat.
DR CTD; 165; -.
DR RGD; 1306922; Aebp1.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158323; -.
DR HOGENOM; CLU_006722_0_1_1; -.
DR InParanoid; A2RUV9; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; A2RUV9; -.
DR TreeFam; TF315592; -.
DR PRO; PR:A2RUV9; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Genevisible; A2RUV9; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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; ISO:RGD.
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 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 2: Evidence at transcript level;
KW Calmodulin-binding; DNA-binding; Glycoprotein; Reference proteome;
KW Repressor; Secreted; Signal; 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_0000333191"
FT DOMAIN 375..532
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 40..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..547
FT /note="Required for DNA-binding and interaction with
FT NFKBIA"
FT /evidence="ECO:0000250"
FT REGION 413..616
FT /note="Interaction with MAPK1 and MAPK3"
FT /evidence="ECO:0000250"
FT REGION 547..977
FT /note="Interaction with PTEN"
FT /evidence="ECO:0000250"
FT REGION 933..1128
FT /note="Required for transcriptional repression"
FT /evidence="ECO:0000250"
FT REGION 998..1128
FT /note="Interaction with MAPK1 and MAPK3"
FT /evidence="ECO:0000250"
FT REGION 1027..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1128 AA; 128061 MW; EC2A4DDC46240A4F CRC64;
MAAVRTASLL CGLLALLALC PEGSPQTVLT DDEIQEFLEG FLSEFETQSP PREDDVEAQP
LPEPTQRARK SKAGGKPRAD AEAPPEKNKD KEKKGKKDKG PKAAKHLEGS TRPTKKPKEK
PPKATKKPKE KPPKATKKPK EKPPKATKKP KEKPPKATKR PSAGKRFSTV APLETPERSL
TSPSNPGTRE LPEERGRTSL NTWQGQGEET QVEARQHRPE PEEETEMPTL DYNDQIERED
YEDFEYIRRQ KQPRPTPSRK RIWPEPPEEK TQEPEERKEV DPPLKPLLPP DYGDGYLIPN
YDDLDYYFPH PPPQKPDVGQ EVDEEKEELK KPKKEGSSPK EDTEDKWAAE KNKDHKAGPR
KGEELEEEWG PVEKIKCPPI GMESHRIEDN QIRASSMLRH GLGAQRGRLN MQAGANEDDY
YDGAWCAEDE SQTQWIEVDT RRTTRFTGVI TQGRDSSIHD DFVTTFFVGF SNDSQTWVMY
TNGYEEMTFH GNVDKDTPVL SELPEPVVAR FIRIYPLTWN GSLCMRLEVL GCPVTPVYSY
YAQNEVVTTD SLDFRHHSYK DMRQLMKVVN EECPTITRTY SLGKSSRGLK IYAMEISDNP
GEHELGEPEF RYTAGMHGNE VLGRELLLLL MQYLCHEYRD GNPRVRNLVQ DTRIHLVPSL
NPDGYEVAAQ MGSEFGNWAL GLWTEEGFDI FEDFPDLNSV LWAAEEKKWV PYRVPNNNLP
IPERYLSPDA TVSTEVRAII SWMEKNPFVL GANLNGGERL VSYPYDMART PSQEQLLAAA
LAAARGEDED EVSEAQETPD HAIFRWLAIS FASAHLTMTE PYRGGCQAQD YTSGMGIVNG
AKWNPRSGTF NDFSYLHTNC LELSIYLGCD KFPHESELPR EWENNKEALL TFMEQVHRGI
KGVVTDEQGI PIANATISVS GINHGVKTAS GGDYWRILNP GEYRVTAHAE GYTSSAKICN
VDYDIGATQC NFILARSNWK RIREILAMNG NRPILRVDPS RPMTPQQRRL QQRRLRYRLR
MREQMRLRRL NSTTGPATSP TPALTLPPSP TPGSTSRLWE ILPTTAAGWE ESETETYTEV
VTEFETEYGP DLEVEELEEE EEEEEEMDTG LTFPVTTVET YTVNFGDF
