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Protein

Adipocyte enhancer-binding protein 1

Gene

Aebp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Calmodulin-binding, DNA-binding

Protein family/group databases

MEROPSiM14.951.

Names & Taxonomyi

Protein namesi
Recommended name:
Adipocyte enhancer-binding protein 1
Short name:
AE-binding protein 1
Alternative name(s):
Aortic carboxypeptidase-like protein
Gene namesi
Name:Aebp1
Synonyms:Aclp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306922. Aebp1.

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 11281103Adipocyte enhancer-binding protein 1PRO_0000333191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylated by MAPK1 in vitro.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiA2RUV9.
PRIDEiA2RUV9.

Expressioni

Tissue specificityi

Expressed in aorta.2 Publications

Developmental stagei

Highly expressed in quiescent cells.1 Publication

Gene expression databases

GenevisibleiA2RUV9. RN.

Interactioni

Subunit structurei

Interacts with GNG5, NFKBIA, MAPK1, MAPK3 and PTEN. May interact with calmodulin. Binds to DNA in vitro.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018846.

Structurei

3D structure databases

ProteinModelPortaliA2RUV9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini375 – 532158F5/8 type CPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni382 – 547166Required for DNA-binding and interaction with NFKBIABy similarityAdd
BLAST
Regioni413 – 616204Interaction with MAPK1 and MAPK3By similarityAdd
BLAST
Regioni547 – 977431Interaction with PTENBy similarityAdd
BLAST
Regioni933 – 1128196Required for transcriptional repressionBy similarityAdd
BLAST
Regioni998 – 1128131Interaction with MAPK1 and MAPK3By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi70 – 15990Lys-richAdd
BLAST
Compositional biasi253 – 31664Pro-richAdd
BLAST
Compositional biasi976 – 102954Arg-richAdd
BLAST
Compositional biasi1070 – 110637Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated
Contains 1 F5/8 type C domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiA2RUV9.
OMAiTLDYNDQ.
OrthoDBiEOG7B8S32.
PhylomeDBiA2RUV9.
TreeFamiTF315592.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF00754. F5_F8_type_C. 1 hit.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
SMARTiSM00231. FA58C. 1 hit.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2RUV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVRTASLL CGLLALLALC PEGSPQTVLT DDEIQEFLEG FLSEFETQSP
60 70 80 90 100
PREDDVEAQP LPEPTQRARK SKAGGKPRAD AEAPPEKNKD KEKKGKKDKG
110 120 130 140 150
PKAAKHLEGS TRPTKKPKEK PPKATKKPKE KPPKATKKPK EKPPKATKKP
160 170 180 190 200
KEKPPKATKR PSAGKRFSTV APLETPERSL TSPSNPGTRE LPEERGRTSL
210 220 230 240 250
NTWQGQGEET QVEARQHRPE PEEETEMPTL DYNDQIERED YEDFEYIRRQ
260 270 280 290 300
KQPRPTPSRK RIWPEPPEEK TQEPEERKEV DPPLKPLLPP DYGDGYLIPN
310 320 330 340 350
YDDLDYYFPH PPPQKPDVGQ EVDEEKEELK KPKKEGSSPK EDTEDKWAAE
360 370 380 390 400
KNKDHKAGPR KGEELEEEWG PVEKIKCPPI GMESHRIEDN QIRASSMLRH
410 420 430 440 450
GLGAQRGRLN MQAGANEDDY YDGAWCAEDE SQTQWIEVDT RRTTRFTGVI
460 470 480 490 500
TQGRDSSIHD DFVTTFFVGF SNDSQTWVMY TNGYEEMTFH GNVDKDTPVL
510 520 530 540 550
SELPEPVVAR FIRIYPLTWN GSLCMRLEVL GCPVTPVYSY YAQNEVVTTD
560 570 580 590 600
SLDFRHHSYK DMRQLMKVVN EECPTITRTY SLGKSSRGLK IYAMEISDNP
610 620 630 640 650
GEHELGEPEF RYTAGMHGNE VLGRELLLLL MQYLCHEYRD GNPRVRNLVQ
660 670 680 690 700
DTRIHLVPSL NPDGYEVAAQ MGSEFGNWAL GLWTEEGFDI FEDFPDLNSV
710 720 730 740 750
LWAAEEKKWV PYRVPNNNLP IPERYLSPDA TVSTEVRAII SWMEKNPFVL
760 770 780 790 800
GANLNGGERL VSYPYDMART PSQEQLLAAA LAAARGEDED EVSEAQETPD
810 820 830 840 850
HAIFRWLAIS FASAHLTMTE PYRGGCQAQD YTSGMGIVNG AKWNPRSGTF
860 870 880 890 900
NDFSYLHTNC LELSIYLGCD KFPHESELPR EWENNKEALL TFMEQVHRGI
910 920 930 940 950
KGVVTDEQGI PIANATISVS GINHGVKTAS GGDYWRILNP GEYRVTAHAE
960 970 980 990 1000
GYTSSAKICN VDYDIGATQC NFILARSNWK RIREILAMNG NRPILRVDPS
1010 1020 1030 1040 1050
RPMTPQQRRL QQRRLRYRLR MREQMRLRRL NSTTGPATSP TPALTLPPSP
1060 1070 1080 1090 1100
TPGSTSRLWE ILPTTAAGWE ESETETYTEV VTEFETEYGP DLEVEELEEE
1110 1120
EEEEEEMDTG LTFPVTTVET YTVNFGDF
Length:1,128
Mass (Da):128,061
Last modified:March 6, 2007 - v1
Checksum:iEC2A4DDC46240A4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133065 mRNA. Translation: AAI33066.1.
RefSeqiNP_001094440.1. NM_001100970.1.
UniGeneiRn.37157.

Genome annotation databases

GeneIDi305494.
KEGGirno:305494.
UCSCiRGD:1306922. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133065 mRNA. Translation: AAI33066.1.
RefSeqiNP_001094440.1. NM_001100970.1.
UniGeneiRn.37157.

3D structure databases

ProteinModelPortaliA2RUV9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018846.

Protein family/group databases

MEROPSiM14.951.

Proteomic databases

PaxDbiA2RUV9.
PRIDEiA2RUV9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi305494.
KEGGirno:305494.
UCSCiRGD:1306922. rat.

Organism-specific databases

CTDi165.
RGDi1306922. Aebp1.

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiA2RUV9.
OMAiTLDYNDQ.
OrthoDBiEOG7B8S32.
PhylomeDBiA2RUV9.
TreeFamiTF315592.

Miscellaneous databases

PROiA2RUV9.

Gene expression databases

GenevisibleiA2RUV9. RN.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF00754. F5_F8_type_C. 1 hit.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
SMARTiSM00231. FA58C. 1 hit.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  2. "Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation."
    Layne M.D., Endege W.O., Jain M.K., Yet S.-F., Hsieh C.-M., Chin M.T., Perrella M.A., Blanar M.A., Haber E., Lee M.-E.
    J. Biol. Chem. 273:15654-15660(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "Gene structure and expression of the mouse adipocyte enhancer-binding protein."
    Ro H.-S., Kim S.-W., Wu D., Webber C., Nicholson T.E.
    Gene 280:123-133(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiAEBP1_RAT
AccessioniPrimary (citable) accession number: A2RUV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 6, 2007
Last modified: June 8, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Although related to peptidase M14 family, lacks the active sites residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.