ID A0A3B6KIL3_WHEAT Unreviewed; 912 AA.
AC A0A3B6KIL3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=CFC21_065702 {ECO:0000313|EMBL:KAF7058699.1};
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:TraesCS5A02G194100.2};
RN [1] {ECO:0000313|EMBL:KAF7058699.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7058699.1};
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:TraesCS5A02G194100.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5A02G194100.2};
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:TraesCS5A02G194100.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7058699.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7058699.1};
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; CM022223; KAF7058699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6KIL3; -.
DR EnsemblPlants; TraesCS5A02G194100.2; TraesCS5A02G194100.2; TraesCS5A02G194100.
DR Gramene; TraesCS5A02G194100.2; TraesCS5A02G194100.2; TraesCS5A02G194100.
DR Gramene; TraesCS5A03G0501000.1; TraesCS5A03G0501000.1.CDS; TraesCS5A03G0501000.
DR Proteomes; UP000019116; Chromosome 5A.
DR Proteomes; UP000815260; Chromosome 5A.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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:SF203; AMINOPEPTIDASE M1-C; 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..912
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040071286"
FT DOMAIN 72..250
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 285..501
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 579..886
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 39..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 442
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 912 AA; 101075 MW; 541397D293344D8B CRC64;
MAPSRAGAGA VLPVVVALLL GVVAAAAATG GARKMASHGE GANLKASPGA PAAGGSADQF
RGKARLPSFA APRRYELFLR PDLVACTFSG SVAISVAVSA PTRFLVLNAL DLSVNRASIR
FQALEPTEVV FFKDDGVLVL GFAKQLPLGE GLLKMDFNGT LNDQMRGFYR SKYQYKGKER
NMAVTQFESV DARRCFPCWD EPAFKAKFKL TLEVPSELVA LSNMPVANAT FAGPIKTVRY
QESPPMSTYL VAIVVGLFEY VEGMTTKGTR VRVYTQIGKS NQGKFALDVG VKSLNLYKDY
FDTPYPLPKL DMIAIPDFAA GAMENYGLVT YREVALLFDD KSSSASSKQS VAITVAHELA
HQWFGNLVTM EWWTHLWLNE GFATWMSHLA VDSFFPQWNI WTQFLDSTTT ALRLDSLEAS
HPIEVEIHHA SEVDQIFDAI SYDKGASVIR MLQSYLGAER FQKAMASYMK KYAYSNAKTE
DLWAVLEKET GEPVKDLMTT WTKQKGYPVI NAKIKGNDIE IEQAQFLLDG SSGSGMWIVP
VTSGCGAYDT QKKFLLKLKR DKLVIDSQCG DRKKGGNFWT KLNINGTGFY RVKYDDELAA
ALQNALETKK LSLMDKIGIV DDLYALSIAR QQTFASLLRL LYGYRGEADY SVLSHINTVT
ASIAKVSADA IPALAGDIKQ LLIKILLSPA EKLGWDPKKG ESHLDVMLRP LLLTALVQLG
YGKTINEGVR RFNIFTRDRS TSLLPPDTRK AAYLSVMQNV SSSNRSGYDA LRKIYKESAE
GEERLQVLGI LSSCRDKSIV LESLNLIFTN EVRNQDASML LRGIQPEARE ISWNWLKENW
ERISRTFSGS LEFTSNEKAA EISKFFATRT KPGFERTLKQ SLESVRISAR WAEGIRSEPG
LAQTVRELLA KP
//
