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Database: UniProt
Entry: A0A0D2U4X3_GOSRA
LinkDB: A0A0D2U4X3_GOSRA
Original site: A0A0D2U4X3_GOSRA 
ID   A0A0D2U4X3_GOSRA        Unreviewed;       479 AA.
AC   A0A0D2U4X3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|PROSITE:PS00631};
GN   ORFNames=B456_013G216000 {ECO:0000313|EMBL:KJB82823.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB82823.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB82823.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001585};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC         is preferably Leu, but may be other amino acids including Pro
CC         although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC         methyl esters are also readily hydrolyzed, but rates on arylamides
CC         are exceedingly low.; EC=3.4.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000135};
CC   -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC       {ECO:0000256|ARBA:ARBA00011867}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CM001752; KJB82823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2U4X3; -.
DR   EnsemblPlants; KJB82823; KJB82823; B456_013G216000.
DR   Gramene; KJB82823; KJB82823; B456_013G216000.
DR   Proteomes; UP000032304; Chromosome 13.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00433; Peptidase_M17; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT   DOMAIN          330..337
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   479 AA;  49892 MW;  951146CEAABDE2B6 CRC64;
     MTKDENSKFQ NPILKKLDGL LGGLLAEASF EEDFTGKAGQ SLVHRLPGLG SKRVGLFGLG
     QSASSPAAFH GLGEAVAAAA KTAQASGVAV ILASSECPSA MSKGNTAAAI VSGTVLGLYE
     DNRYKSESKK PQLKSLDILG LGTGPEIEKK IKYAEVVSCA IIFGRELVNS PANVLTPAAL
     AAEASKIASL YSDVLSANIL TEEQCRELKM GSYLGVAAAS ANPPHFIHLC YKPPSGPVKT
     KLALVGKGLT FDSGGYNIKT GPGCSIETMK ADMGGSAAVF GAAKALGQIK PSGVEVHFIV
     ASCENMISGK GMRPGDIVTA SNGKTIEVNN TDAEGRLTLA DALVYACNQG VEKIVDLATL
     TGACVVALGP SIAGIFTPND DLAKELFQAS EASGEKFWRM PLEESYWESM KSGVADMVNT
     GGRQGGAINA ALFLKQFVDE KVKWMHIDMA GPVLNDKKHV ATGFGISTLV EWVLKNSSS
//
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