LOCUS       NP_001120               1158 aa            linear   PRI 27-APR-2025
DEFINITION  adipocyte enhancer-binding protein 1 precursor [Homo sapiens].
ACCESSION   NP_001120
VERSION     NP_001120.3
DBSOURCE    REFSEQ: accession NM_001129.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Liu,S., Gu,Y., Shi,Y., Yu,S., Li,W. and Lv,W.
  TITLE     AEBP1 upregulation contributes to cervical cancer progression by
            facilitating cell proliferation, migration, and invasion
  JOURNAL   J Obstet Gynaecol Res 50 (7), 1166-1174 (2024)
   PUBMED   38684171
  REMARK    GeneRIF: AEBP1 upregulation contributes to cervical cancer
            progression by facilitating cell proliferation, migration, and
            invasion.
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Asadie,M., Miri,A., Badri,T., Hosseini Nejad,J. and Gharechahi,J.
  TITLE     Dysregulated AEBP1 and COLEC12 Genes in Late-Onset Alzheimer's
            Disease: Insights from Brain Cortex and Peripheral Blood Analysis
  JOURNAL   J Mol Neurosci 74 (2), 37 (2024)
   PUBMED   38568322
  REMARK    GeneRIF: Dysregulated AEBP1 and COLEC12 Genes in Late-Onset
            Alzheimer's Disease: Insights from Brain Cortex and Peripheral
            Blood Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Ju,G., Xing,T., Xu,M., Zhang,X., Sun,Y., Mu,Z., Sun,D., Miao,S.,
            Li,L., Liang,J. and Lin,Y.
  TITLE     AEBP1 promotes papillary thyroid cancer progression by activating
            BMP4 signaling
  JOURNAL   Neoplasia 49, 100972 (2024)
   PUBMED   38237535
  REMARK    GeneRIF: AEBP1 promotes papillary thyroid cancer progression by
            activating BMP4 signaling.
REFERENCE   4  (residues 1 to 1158)
  AUTHORS   Corano Scheri,K., Lavine,J.A., Tedeschi,T., Thomson,B.R. and
            Fawzi,A.A.
  TITLE     Single-cell transcriptomics analysis of proliferative diabetic
            retinopathy fibrovascular membranes reveals AEBP1 as fibrogenesis
            modulator
  JOURNAL   JCI Insight 8 (23), e172062 (2023)
   PUBMED   37917183
  REMARK    GeneRIF: Single-cell transcriptomics analysis of proliferative
            diabetic retinopathy fibrovascular membranes reveals AEBP1 as
            fibrogenesis modulator.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1158)
  AUTHORS   Li,Y.X., Zhu,X.X., Wu,X., Li,J.H., Ni,X.H., Li,S.J., Zhao,W. and
            Yin,X.Y.
  TITLE     ACLP promotes activation of cancer-associated fibroblasts and tumor
            metastasis via ACLP-PPARgamma-ACLP feedback loop in pancreatic
            cancer
  JOURNAL   Cancer Lett 544, 215802 (2022)
   PUBMED   35732215
  REMARK    GeneRIF: ACLP promotes activation of cancer-associated fibroblasts
            and tumor metastasis via ACLP-PPARgamma-ACLP feedback loop in
            pancreatic cancer.
REFERENCE   6  (residues 1 to 1158)
  AUTHORS   Layne,M.D., Yet,S.F., Maemura,K., Hsieh,C.M., Bernfield,M.,
            Perrella,M.A. and Lee,M.E.
  TITLE     Impaired abdominal wall development and deficient wound healing in
            mice lacking aortic carboxypeptidase-like protein
  JOURNAL   Mol Cell Biol 21 (15), 5256-5261 (2001)
   PUBMED   11438679
  REMARK    GeneRIF: Most ACLP knockout mice die perinatally due to abdominal
            issues.
REFERENCE   7  (residues 1 to 1158)
  AUTHORS   Muise,A.M. and Ro,H.S.
  TITLE     Enzymic characterization of a novel member of the regulatory B-like
            carboxypeptidase with transcriptional repression function:
            stimulation of enzymic activity by its target DNA
  JOURNAL   Biochem J 343 Pt 2 (Pt 2), 341-345 (1999)
   PUBMED   10510298
REFERENCE   8  (residues 1 to 1158)
  AUTHORS   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. and Lee,M.E.
  TITLE     Aortic carboxypeptidase-like protein, a novel protein with
            discoidin and carboxypeptidase-like domains, is up-regulated during
            vascular smooth muscle cell differentiation
  JOURNAL   J Biol Chem 273 (25), 15654-15660 (1998)
   PUBMED   9624159
REFERENCE   9  (residues 1 to 1158)
  AUTHORS   Song,L. and Fricker,L.D.
  TITLE     Cloning and expression of human carboxypeptidase Z, a novel
            metallocarboxypeptidase
  JOURNAL   J Biol Chem 272 (16), 10543-10550 (1997)
   PUBMED   9099699
REFERENCE   10 (residues 1 to 1158)
  AUTHORS   Ohno,I., Hashimoto,J., Shimizu,K., Takaoka,K., Ochi,T.,
            Matsubara,K. and Okubo,K.
  TITLE     A cDNA cloning of human AEBP1 from primary cultured osteoblasts and
            its expression in a differentiating osteoblastic cell line
  JOURNAL   Biochem Biophys Res Commun 228 (2), 411-414 (1996)
   PUBMED   8920928
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006454.4, BC038588.1 and
            DB213495.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 1, 2004 this sequence version replaced NP_001120.2.
            
            Summary: This gene encodes a member of carboxypeptidase A protein
            family. The encoded protein may function as a transcriptional
            repressor and play a role in adipogenesis and smooth muscle cell
            differentiation. Studies in mice suggest that this gene functions
            in wound healing and abdominal wall development. Overexpression of
            this gene is associated with glioblastoma. [provided by RefSeq, May
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038588.1, AB209744.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223357.8/ ENSP00000223357.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1158
                     /product="adipocyte enhancer-binding protein 1 precursor"
                     /note="aortic carboxypeptidase-like protein; adipocyte
                     enhancer-binding protein 1"
                     /calculated_mol_wt=128483
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2464
     mat_peptide     26..1158
                     /product="Adipocyte enhancer-binding protein 1.
                     /id=PRO_0000333189"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
                     /calculated_mol_wt=128483
     Region          41..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          386..539
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Region          390..555
                     /region_name="Required for DNA-binding and interaction
                     with NFKBIA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          421..624
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Site            order(434,462,469)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          555..985
                     /region_name="Interaction with PTEN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          564..903
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Site            order(625,628,690,699..700,763..764,770,874)
                     /site_type="active"
                     /db_xref="CDD:349441"
     Region          907..982
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cd11308"
                     /db_xref="CDD:200604"
     Site            922
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          941..1158
                     /region_name="Required for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          1006..1158
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          1108..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     CDS             1..1158
                     /gene="AEBP1"
                     /gene_synonym="ACLP"
                     /coded_by="NM_001129.5:322..3798"
                     /db_xref="CCDS:CCDS5476.1"
                     /db_xref="GeneID:165"
                     /db_xref="HGNC:HGNC:303"
                     /db_xref="MIM:602981"
ORIGIN      
        1 maavrgapll scllallalc pggrpqtvlt ddeieefleg flselepepr eddveapppp
       61 eptprvrkaq aggkpgkrpg taaevppekt kdkgkkgkkd kgpkvpkesl egsprppkkg
      121 kekppkatkk pkekppkatk kpkekppkat kkpkekppka tkkppsgkrp pilapsetle
      181 wplppppspg peelpqegga plsnnwqnpg eethveareh qpepeeeteq ptldyndqie
      241 redyedfeyi rrqkqprppp srrrrpervw peppeekapa papeeriepp vkpllpplpp
      301 dygdgyvipn yddmdyyfgp pppqkpdaer qtdeekeelk kpkkedsspk eetdkwavek
      361 gkdhkeprkg eeleeewtpt ekvkcppigm eshriednqi rassmlrhgl gaqrgrlnmq
      421 tgateddyyd gawcaeddar tqwievdtrr ttrftgvitq grdssihddf vttffvgfsn
      481 dsqtwvmytn gyeemtfhgn vdkdtpvlse lpepvvarfi riypltwngs lcmrlevlgc
      541 svapvysyya qnevvatddl dfrhhsykdm rqlmkvvnee cptitrtysl gkssrglkiy
      601 ameisdnpge helgepefry tagihgnevl grelllllmq ylcreyrdgn prvrslvqdt
      661 rihlvpslnp dgyevaaqmg sefgnwalgl wteegfdife dfpdlnsvlw gaeerkwvpy
      721 rvpnnnlpip erylspdatv stevraiiaw meknpfvlga nlnggerlvs ypydmartpt
      781 qeqllaaama aargededev seaqetpdha ifrwlaisfa sahltltepy rggcqaqdyt
      841 ggmgivngak wnprtgtind fsylhtncle lsfylgcdkf pheselprew ennkealltf
      901 meqvhrgikg vvtdeqgipi anatisvsgi nhgvktasgg dywrilnpge yrvtahaegy
      961 tpsaktcnvd ydigatqcnf ilarsnwkri reimamngnr piphidpsrp mtpqqrrlqq
     1021 rrlqhrlrlr aqmrlrrlna tttlgphtvp ptlppapatt lsttiepwgl ippttagwee
     1081 setetytevv tefgtevepe fgtkvepefe tqlepefetq lepefeeeee eekeeeiatg
     1141 qafpfttvet ytvnfgdf
//
