ID A0A1U7XHW6_NICSY Unreviewed; 886 AA.
AC A0A1U7XHW6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Puromycin-sensitive aminopeptidase isoform X4 {ECO:0000313|RefSeq:XP_009786065.1};
GN Name=LOC104234223 {ECO:0000313|RefSeq:XP_009786065.1};
OS Nicotiana sylvestris (Wood tobacco) (South American 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=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009786065.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009786065.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009786065.1};
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_009786065.1; XM_009787763.1.
DR AlphaFoldDB; A0A1U7XHW6; -.
DR GeneID; 104234223; -.
DR OrthoDB; 745at2759; -.
DR Proteomes; UP000189701; 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_009786065.1};
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:UP000189701};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 23..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..439
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 447..560
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 564..885
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 886 AA; 99884 MW; CD00116E2F3A214D CRC64;
MEAPKEIFLK DYKQPDYYFD TVDLKFSLGE ESTFVASKIA VSPRVEGQSF PLVLNGQDLK
LQSIKINGNP LKEEDFHLDS RHLTLKSPPS SKFTLEIVTE IYPQKNTSLE GLYKSSGNFC
TQCEAEGFRK ITFYQDRPDI MAKYTCRIEA DKSLYPVLLS NGNLIEQGDL EGGKHFTVWE
DPFKKPCYLF ALVAGQLESR DDTFITRSGR NVSLRIWTPA QDLPKTAHAM YSLKAAMKWD
EDVFGLEYDL DLFNIVAVPD FNMGAMENKS LNIFNSKLVL ASPETATDAD YAAILGVIGH
EYFHNWTGNR VTCRDWFQLS LKEGLTVFRD QEFSSDMGSR TVKRIADVSK LRMYQYPQDS
GPMAHPVRPH SYIKMDNFYT VTVYEKGAEV VRMYKTLLGS QGFRKGMDLY FMRHDGQAVT
CEDFFAAMRD ANNADFANFL LWYSQAGTPV VKVATNYSAE SRTFSLKFSQ EVPPTPGQSA
KEPMFIPVAV GLLDSSGKDM PLSSVYHDGK LESFASSGQN VHTTVLRITK KEEEFVFNDI
SEKPTPSILR GFSAPIRLES DLTDSDLLFL LAHDSDEFNR WEAGQVLARK LMLSLVADFQ
QNKALVLNPQ FVQGIKSILT DSSLDKEFIA KAITLPGVGE IMDMMTVADP DAVHAVRTFI
RKQLASELKE ELLITAKNNR SSGAYEFDHN NMARRALKNT ALAYLGSLEG PEITELLLNE
YRNATNMTDQ FSALVAIDQQ PAIREEILAD FYNKWQDDFL VVNKWFALQA MSDVPGNVEN
VKKLLNHTAF DLRNPNKVYS LIGGFCGSPV NFHCKDGSGY KFLGELVVQL DKINPQVASR
MVSAFSRWKR YDETRQSLAK EQLEMILSTE GLSENVFEIA SKSLAA
//
