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Database: UniProt
Entry: V4P368_EUTSA
LinkDB: V4P368_EUTSA
Original site: V4P368_EUTSA 
ID   V4P368_EUTSA            Unreviewed;       879 AA.
AC   V4P368;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=EUTSA_v10024371mg {ECO:0000313|EMBL:ESQ53846.1};
OS   Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX   NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ53846.1, ECO:0000313|Proteomes:UP000030689};
RN   [1] {ECO:0000313|EMBL:ESQ53846.1, ECO:0000313|Proteomes:UP000030689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA   Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA   Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA   Mitchell-Olds T., Schumaker K.S., Wang X.;
RT   "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL   Front. Plant Sci. 4:46-46(2013).
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: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Microsome
CC       membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR   EMBL; KI517384; ESQ53846.1; -; Genomic_DNA.
DR   RefSeq; XP_006412393.1; XM_006412330.1.
DR   AlphaFoldDB; V4P368; -.
DR   STRING; 72664.V4P368; -.
DR   MEROPS; M01.A25; -.
DR   EnsemblPlants; ESQ53846; ESQ53846; EUTSA_v10024371mg.
DR   GeneID; 18029734; -.
DR   Gramene; ESQ53846; ESQ53846; EUTSA_v10024371mg.
DR   KEGG; eus:EUTSA_v10024371mg; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   OMA; MMEYVAI; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000030689; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010013; F:N-1-naphthylphthalamic acid binding; IEA:EnsemblPlants.
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; 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; 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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU364040};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU364040}; Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030689};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          15..200
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          235..451
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          536..854
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        308
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            392
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   879 AA;  98043 MW;  98C17FD73DC6691A CRC64;
     MDQFKGQPRL PKFAVPKRYD LRLNPDLSAC TFSGTVAIDL DIVADTRFIV LNAADLSVND
     ASVSFTPPTS SKALAAPKVS LFEEDEIMVL EFGEILPHGV GVLQMGFNGV LNDKMKGFYK
     STYEHNGEKK NMAVTQFEPA DARRCFPCWD EPACKATFKI TLEVPTELVA LSNMPVMEEK
     VNGNLKIVSY QESPIMSTYL VAIVVGLFDY VEDHTSDGIK VRVYCQVGKA DQGKFALDVG
     AKTLDLFKEY FAVPYPLPKM DMIAIPDFAA GAMENYGLVT YRETALLYDE QHSAASNKQR
     VATVVAHELA HQWFGNLVTM EWWTHLWLNE GFATWVSYLA TDSLFPEWEI WTQFLDESTE
     GLRLDGLEES HPIEVEVNHA AEIDEIFDAI SYRKGASVIR MLQSYLGAEV FQKSLAAYIK
     NHAYSNAKTE DLWTALEGGS GEPVNKLMSS WTKQKGYPVV SAKIKDGKLE LEQSRFLSSG
     SPGEGQWIVP VTLCCGSYDM RKNFLLESKS GAYDLKELLG CSIADGSGKT NATCSWIKIN
     VDQAGFYRVK YDDSLAAGLR NATESKSLTS IDRYGILDDS FALSMALQQS LASLLTLISA
     YKKELDYTVL SNLIVISYKV VKIGADANLE LMSAIKQFFI GVFQFAAGKL GWDPKQGESH
     LDAMLRGEIL TALAVFGHEE TLKEAVRRFD AFLADRNTSL LPPDLRRAAY VAVMQRANKS
     DKSGYESLLR VYRETDLSQE KTRILGTLAS CPDPDVVQDV LNFVLSDEVR NQDALYGLSG
     VSWEGREVAW KWLKEKWEYI GATWGSGFLI TRFISAVVSP FASIEKAKEA EEFFATRSKP
     SMARTLKQSI ERVHINANWV ESIRKEDNLT QLVAQLSQN
//
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