ID A0A1S3Z2B1_TOBAC Unreviewed; 977 AA.
AC A0A1S3Z2B1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Puromycin-sensitive aminopeptidase-like isoform X3 {ECO:0000313|RefSeq:XP_016458555.1};
GN Name=LOC107782212 {ECO:0000313|RefSeq:XP_016458555.1};
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_016458555.1};
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_016458555.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_016458555.1; XM_016603069.1.
DR AlphaFoldDB; A0A1S3Z2B1; -.
DR GeneID; 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_016458555.1};
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 114..280
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 321..530
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 538..651
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 655..976
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 977 AA; 110230 MW; B1404193C32F34C1 CRC64;
MARLVLPCKP SSLSKTCLLG LISNAPASCR VASVVRSRNI CRYKQYISSE VTHWRRCQIP
RFPLVQPRRT DRRLICSVAT EPLPKEVEET KMAAPKEIFL KDYKQPDYYF DTVDLKFSLG
EESTFVASKI AVSPRVEGQS FPLVLNGQDL KLQSIKINGN PLKEEDFHLD SRHLTLKSPP
SSKFTLEIVT EIYPQKNTSL EGLYKSSGNF CTQCEAEGFR KITFYQDRPD IMAKYTCRIE
ADKSLYPVLL SNGNLIEQGD LEGGKHFTVW EDPFKKPCYL FALVAGQLES RDDTFTTRSG
RNVSLRIWTP AQDLPKTAHA MYSLKAAMKW DEDVFGLEYD LDLFNIVAVP DFNMGAMENK
SLNIFNSKLV LASPETATDA DYAAILGVIG HEYFHNWTGN RVTCRDWFQL SLKEGLTVFR
DQEFSSDMGS RTVKRIADVS KLRMYQYPQD SGPMAHPVRP HSYIKMDNFY TVTVYEKGAE
VVRMYKTLLG SQGFRKGMDL YFKRHDGQAV TCEDFFAAMR DANNADFANF LLWYSQAGTP
VVKVTTNYNA ESHTFSLKFS QEVPPTPGQS AKEPMFIPVA VGLLDSSGKD MPLSSVYHEG
KLESFTSSGQ NVHTTVLRIT KKEEEFVFND ISEKPTPSIL RGFSAPIRLE SDLTDSDLLF
LLAHDSDEFN RWEAGQVLAR KLMLSLVADF QQNKALVLNP QFVQGIKSIL TDSSLDKEFI
AKAITLPGVG EIMDMMTVAD PDAVHAVRTF IRKQLASELK EDLLITTKNN RSSGAYEFDH
NNMARRALKN IALAYLGSLE GPEITELLLN EYSNATNMTD QFSALVAIDQ QPAIREEILA
DFYNKWQDDF LVVNKWFALQ AMSDVPGNVE NVKKLLNHTA FDLRNPNKVY SLIGGFCGSP
VNFHCKDGSG YKFLGELVVQ LDKINPQVAS RMVSAFSRWK RYDETRQSLA KEQLEMILST
EGLSENVFEI ASKSLAA
//
