ID E2ARG9_CAMFO Unreviewed; 831 AA.
AC E2ARG9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=PEST proteolytic signal-containing nuclear protein {ECO:0000256|ARBA:ARBA00022059};
GN ORFNames=EAG_09591 {ECO:0000313|EMBL:EFN63978.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN63978.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- FUNCTION: May be involved in cell cycle regulation.
CC {ECO:0000256|ARBA:ARBA00002646}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Interacts with UHRF2/NIRF. {ECO:0000256|ARBA:ARBA00011097}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL442063; EFN63978.1; -; Genomic_DNA.
DR AlphaFoldDB; E2ARG9; -.
DR EnsemblMetazoa; XM_011264403.3; XP_011262705.1; LOC105255237.
DR InParanoid; E2ARG9; -.
DR OMA; CITMANH; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR029169; PCNP.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF276; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF15473; PCNP; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Aminopeptidase {ECO:0000313|EMBL:EFN63978.1};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..79
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 170..350
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 454..744
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 831 AA; 98220 MW; 333554AFACF52D85 CRC64;
MNRLNFDRWL IATDFQFINA RRMLPCWDKP ALKATFHIAI KHHKNYTALS NMPVRKLHEG
RNNMTWTIFH DTPEMPIYLV AIVLCKDPFL STRILHEELT FPHIKFKQIL LKDFILNSPI
PNYYGDLNRV TNNWYEQYSV QIRFAQIIAE SVSQLFRIEW TLSLLNIEMI TKIDHIAISD
LRDDSIQYWG LIFYRKANII YREHRDPVAR KFDVARLVAR EITHQWFGNM VSPSSWSYLW
MNDGIAILLG MDTINKIFEK LRILDLFVVQ IQHESLHLDT DFLIKPLISE VNNPSEIDPF
SRFIKAPVIL RMLYMLLNDA FRKGIERYVI NHQFRSAVPN DLWIAIQTEI TYSYVHISPR
VIDTPIINVS LIIDAWTNQM HYPILNVKRD YFDAKEVTIS VENNISEQDN WFIFVTITTE
TEHDFTNFLR AYWIKLTPKS YPYIILTQQK ENDWIIVNLQ QIGYYRVNYD PENWHKIANY
LNSRQYSNIH ILNRAQIIDD AFHLMESGKL HSSIFWKLTS YLKREKDYIA WYPMIKAFEY
MSRIFLLTSF GKVTEIKKNM GNILYTVLQK IGYDEVSVDN DFTKCLIQEA AKWACTFELP
DCINTAHHKL THHLKDDFGK NELMPWWRKW TYCKGMMIAS FETWLKTLNL WKKTQDNKIL
DYLTCTNNFE IIFSYLSRTM NEHDFKSTTI LFQATEHISI FFSIVAKHAR NNEILEYILN
NFKAIKPRET STIAALTHII NNVYTKEQLE KKPSPKATTV QKPTVASVFN TDEDDEPEEM
PAEARMRMRN IGRETPTSAG PNSFGKTKQG FCDSKKIFEK TLKKAMEEAN K
//
