ID A0A1S3Z262_TOBAC Unreviewed; 979 AA.
AC A0A1S3Z262;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Puromycin-sensitive aminopeptidase-like isoform X1 {ECO:0000313|RefSeq:XP_016458551.1, ECO:0000313|RefSeq:XP_016458552.1};
GN Name=LOC107782212 {ECO:0000313|RefSeq:XP_016458551.1,
GN ECO:0000313|RefSeq:XP_016458552.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016458551.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016458551.1, ECO:0000313|RefSeq:XP_016458552.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR RefSeq; XP_016458551.1; XM_016603065.1.
DR RefSeq; XP_016458552.1; XM_016603066.1.
DR STRING; 4097.A0A1S3Z262; -.
DR PaxDb; 4097-A0A1S3Z262; -.
DR GeneID; 107782212; -.
DR KEGG; nta:107782212; -.
DR OrthoDB; 745at2759; -.
DR Proteomes; UP000084051; Unplaced.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:0000313|RefSeq:XP_016458551.1,
KW ECO:0000313|RefSeq:XP_016458552.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 116..282
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 323..532
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 540..653
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 657..978
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 979 AA; 110505 MW; EA263E8F14C5E257 CRC64;
MARLVLPCKP SSLSKTCLLG LISNAPFQAS CRVASVVRSR NICRYKQYIS SEVTHWRRCQ
IPRFPLVQPR RTDRRLICSV ATEPLPKEVE ETKMAAPKEI FLKDYKQPDY YFDTVDLKFS
LGEESTFVAS KIAVSPRVEG QSFPLVLNGQ DLKLQSIKIN GNPLKEEDFH LDSRHLTLKS
PPSSKFTLEI VTEIYPQKNT SLEGLYKSSG NFCTQCEAEG FRKITFYQDR PDIMAKYTCR
IEADKSLYPV LLSNGNLIEQ GDLEGGKHFT VWEDPFKKPC YLFALVAGQL ESRDDTFTTR
SGRNVSLRIW TPAQDLPKTA HAMYSLKAAM KWDEDVFGLE YDLDLFNIVA VPDFNMGAME
NKSLNIFNSK LVLASPETAT DADYAAILGV IGHEYFHNWT GNRVTCRDWF QLSLKEGLTV
FRDQEFSSDM GSRTVKRIAD VSKLRMYQYP QDSGPMAHPV RPHSYIKMDN FYTVTVYEKG
AEVVRMYKTL LGSQGFRKGM DLYFKRHDGQ AVTCEDFFAA MRDANNADFA NFLLWYSQAG
TPVVKVTTNY NAESHTFSLK FSQEVPPTPG QSAKEPMFIP VAVGLLDSSG KDMPLSSVYH
EGKLESFTSS GQNVHTTVLR ITKKEEEFVF NDISEKPTPS ILRGFSAPIR LESDLTDSDL
LFLLAHDSDE FNRWEAGQVL ARKLMLSLVA DFQQNKALVL NPQFVQGIKS ILTDSSLDKE
FIAKAITLPG VGEIMDMMTV ADPDAVHAVR TFIRKQLASE LKEDLLITTK NNRSSGAYEF
DHNNMARRAL KNIALAYLGS LEGPEITELL LNEYSNATNM TDQFSALVAI DQQPAIREEI
LADFYNKWQD DFLVVNKWFA LQAMSDVPGN VENVKKLLNH TAFDLRNPNK VYSLIGGFCG
SPVNFHCKDG SGYKFLGELV VQLDKINPQV ASRMVSAFSR WKRYDETRQS LAKEQLEMIL
STEGLSENVF EIASKSLAA
//
