ID A0A1D2MU59_ORCCI Unreviewed; 864 AA.
AC A0A1D2MU59;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=Ocin01_10056 {ECO:0000313|EMBL:ODM96620.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM96620.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM96620.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM96620.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
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}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM96620.1}.
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DR EMBL; LJIJ01000520; ODM96620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2MU59; -.
DR STRING; 48709.A0A1D2MU59; -.
DR OMA; RIRANIM; -.
DR OrthoDB; 3256841at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 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; IPR034016; M1_APN-typ.
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; 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 Aminopeptidase {ECO:0000256|RuleBase:RU364040,
KW ECO:0000313|EMBL:ODM96620.1}; Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 39..210
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 249..476
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 561..832
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 409
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 864 AA; 98551 MW; 5F236390BA8B0064 CRC64;
MITVPKHRLH KSVIPQKYFL TIVPILDPGF EDVLGAQWEA PGSVLVNAFA AKATKTITLH
AKNITIHNVT VIHKSEVIPV RNVSQHDRFS FMKIHLSQSL IPGDLYLINI SFTSYVSEVL
NGLFRSSYTN EDTGEQEWFA ATHMEALHAR QMFPCFDEPN LKAVMQAKIG RREDYVALFN
TESTGNETMQ GVDGWVWETF APTVQMSTYL TAMIVAKFQY SEAPGKLLPE TRVRTYAPSH
YIKQGAAVYS AEVAERILST YGEYFKEKYP MKKFDCVAVP SFLYGAMENY GLSIFRETLL
LHFNHSTESK RYIVTNVISH ELGHQWFGNL VSPEWWTNLW LSEGLTKFLE YIGMNATIPE
FEPWDIFISE SLQLGLRLDA DPRTSHSLKI DEDAWLMKNE MEWFDDIAYK KGGSLIRMMQ
GFLSEPVMRK GLSRYLARMK YKSAVQDDLF ADCDKEGQLA HKLPENTTLK DVMSGWTLQA
GFPLLRAKLN GENNVTVSQE KYISIRGSGS ERKMRWFIPV SIATARHPNF DPEPEFWIRN
NETSVELRLP ANSWLILNAG NTEYIPIQNA LNLTKYMKDH AETEQVVWTS LLSMMKTAFK
LFKETDDEFT PLKKYMLPRI EKAIQATGGF DAIKMNSTGM PVLRHAQLLD WACNLYSRGC
IQYAMELVKS WKNTGQLTVP KDFQTVIFSA AVASDSSGEI FDFIKQQYKT AEDTLKDQLL
TALSHSQDTG RIKSLLNEIT KRDLLGDNSE ALVLLQHLGS NAKAADITLQ YFIENFATII
NHFGGINPIV VAANAMAPHL KSLSGLFFID QLVQLNTELF KTSLAPAVSR IRANIMWFDD
FGEDMLEFFE QNSIYQRDFY KRRV
//