ID A0A3B6QGJ4_WHEAT Unreviewed; 877 AA.
AC A0A3B6QGJ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=CFC21_092465 {ECO:0000313|EMBL:KAF7089504.1}, CFC21_092466
GN {ECO:0000313|EMBL:KAF7089507.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6D02G171800.1};
RN [1] {ECO:0000313|EMBL:KAF7089504.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7089504.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6D02G171800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6D02G171800.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS6D02G171800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7089504.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7089504.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM022228; KAF7089504.1; -; Genomic_DNA.
DR EMBL; CM022228; KAF7089507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6QGJ4; -.
DR SMR; A0A3B6QGJ4; -.
DR STRING; 4565.A0A3B6QGJ4; -.
DR PaxDb; 4565-Traes_6DS_CDCAD6797-1; -.
DR EnsemblPlants; TraesCS6D02G171800.1; TraesCS6D02G171800.1; TraesCS6D02G171800.
DR Gramene; TraesCAD_scaffold_092558_01G000100.1; TraesCAD_scaffold_092558_01G000100.1; TraesCAD_scaffold_092558_01G000100.
DR Gramene; TraesCLE_scaffold_003702_01G000300.1; TraesCLE_scaffold_003702_01G000300.1; TraesCLE_scaffold_003702_01G000300.
DR Gramene; TraesCS6D02G171800.1; TraesCS6D02G171800.1; TraesCS6D02G171800.
DR Gramene; TraesCS6D03G0385000.2; TraesCS6D03G0385000.2.CDS; TraesCS6D03G0385000.
DR Gramene; TraesKAR6D01G0128650.1; cds.TraesKAR6D01G0128650.1; TraesKAR6D01G0128650.
DR Gramene; TraesPAR_scaffold_075452_01G000100.1; TraesPAR_scaffold_075452_01G000100.1; TraesPAR_scaffold_075452_01G000100.
DR Gramene; TraesROB_scaffold_038500_01G000100.1; TraesROB_scaffold_038500_01G000100.1; TraesROB_scaffold_038500_01G000100.
DR Gramene; TraesWEE_scaffold_084083_01G000100.1; TraesWEE_scaffold_084083_01G000100.1; TraesWEE_scaffold_084083_01G000100.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000019116; Chromosome 6D.
DR Proteomes; UP000815260; Chromosome 6D.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF282; AMINOPEPTIDASE M1-A; 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 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:UP000019116};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 22..206
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 241..457
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 534..851
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 398
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 877 AA; 98203 MW; 3A1AE0B470464DB3 CRC64;
MAAEQSAEHF RGQARLPGFA APRRYDLRLT PDLAACTFAG SVSVSVDVAA PTRFLVVNAA
DLDVSPGDVH FAPKGSGQVL LPVEVTSALE DEILIIRFNE VLPLGEGTLV IAFQGTLNDK
MKGFYRSVYE LNGEKKNMAV TQFEPADARR CFPCWDEPSF KAVFKITLEV PCETVALSNM
PVVEEKVNGP TKTVYFQESP IMSTYLVAVI VGMFDYVEAF TADGTSVRVY TQVGKSAQGK
FALEVAVKTL ILFKEYFAVP YPLPKMDMIA IPDFASGAME NYGLVTYRET ALLFDERHSA
AANKQRVAVV VAHELAHQWF GNLVTMEWWT HLWLNEGFAT WVSYLAADRF FPEWNVWIQF
LEESTTGFRL DALAGSHPIE VDVNHVDEID EIFDAISYRK GAAVIRMLQS YLGAEIFQKS
LAAYIKRFAY SNAKTEDLWA ALEEGSGEPV KTLMHSWTKQ QGYPVVSVKL KDGKLELEQT
QFLSSGSEGV GQWVVPITLC CCSYSVQQKF LFRGKQDDFN LSGLVECQKK DDFWIKLNVD
QTGFYRVSYD EELASRLRHA VETNILSAAD RYGVLDDTYA LCMAGKQKLV TLLHLIAAYK
NETEYTVLAH AINTSLSIYE MMAVAAPEEL VNMKKFLIDF LEPFAQRVGW DAKSGEGHLN
ALLRGTLLSA LAELGHQSTI DEAVRRFNVF LEDRETPLLP PDVRKAAYVA LMQTVNKSNK
SGYESLLKIY RETDLSQEKV RVLGSLASSP DPDVVREALN FLLSSEVRNQ DCIFVLRGVT
AAAHEVAWTW LKENWDYIAE TFTGHLLTYF ITVTVSPLAT DEKGDEAEEF FKSRTKASIA
RTVKQSIERV RIKAKWVMST KGEADLGNVL KELAHKH
//
