ID A0A1B0CGE2_LUTLO Unreviewed; 1954 AA.
AC A0A1B0CGE2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Puromycin-sensitive aminopeptidase {ECO:0008006|Google:ProtNLM};
OS Lutzomyia longipalpis (Sand fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Lutzomyia; Lutzomyia.
OX NCBI_TaxID=7200 {ECO:0000313|EnsemblMetazoa:LLOJ003443-PA, ECO:0000313|Proteomes:UP000092461};
RN [1] {ECO:0000313|Proteomes:UP000092461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jacobina {ECO:0000313|Proteomes:UP000092461};
RA Richards S., Qu C., Dillon R., Worley K., Scherer S., Batterton M.,
RA Taylor A., Hawes A., Hernandez B., Kovar C., Mandapat C., Pham C., Qu C.,
RA Jing C., Bess C., Bandaranaike D., Ngo D., Ongeri F., Arias F., Lara F.,
RA Weissenberger G., Kamau G., Han H., Shen H., Dinh H., Khalil I., Jones J.,
RA Shafer J., Jayaseelan J., Quiroz J., Blankenburg K., Nguyen L., Jackson L.,
RA Francisco L., Tang L.-Y., Pu L.-L., Perales L., Lorensuhewa L.,
RA Munidasa M., Coyle M., Taylor M., Puazo M., Firestine M., Scheel M.,
RA Javaid M., Wang M., Li M., Tabassum N., Saada N., Osuji N., Aqrawi P.,
RA Fu Q., Thornton R., Raj R., Goodspeed R., Mata R., Najjar R., Gubbala S.,
RA Lee S., Denson S., Patil S., Macmil S., Qi S., Matskevitch T.,
RA Palculict T., Mathew T., Vee V., Velamala V., Korchina V., Cai W., Liu W.,
RA Dai W., Zou X., Zhu Y., Zhang Y., Wu Y.-Q., Xin Y., Nazarath L., Kovar C.,
RA Han Y., Muzny D., Gibbs R.;
RT "Whole Genome Assembly of Lutzomyia longipalpis.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:LLOJ003443-PA}
RP IDENTIFICATION.
RC STRAIN=Jacobina {ECO:0000313|EnsemblMetazoa:LLOJ003443-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; AJWK01011046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01011047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EnsemblMetazoa; LLOJ003443-RA; LLOJ003443-PA; LLOJ003443.
DR VEuPathDB; VectorBase:LLOJ003443; -.
DR OrthoDB; 3264783at2759; -.
DR Proteomes; UP000092461; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; 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; cd09601; M1_APN-Q_like; 2.
DR Gene3D; 1.25.50.20; -; 3.
DR Gene3D; 2.60.40.1910; -; 2.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 2.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 2.
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:SF284; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 3.
DR Pfam; PF01433; Peptidase_M1; 2.
DR Pfam; PF17900; Peptidase_M1_N; 2.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1954
FT /note="Puromycin-sensitive aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008405732"
FT DOMAIN 48..240
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 275..497
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 576..893
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 930..1006
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 1048..1252
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 1342..1610
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 1615..1760
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 436
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1954 AA; 224001 MW; 6034895B3D8FC94B CRC64;
MSPRVAIFLA LIALATATTP HGERNPPEED FSPKQGGAEY RLPTNVLPDS YVVTVTPYLY
AEGGNSEWTF DGNVRINLRA ITDGVTQIVL HATSLEIDNT RSSLRLGGGA QNFLSGTPTY
NNQTAKLTFT TTSALTRDAI YTLELHYKGQ IHNDMRGLYR STYQEGQTTK RLASTQFQTT
FARRFMPCFD EPSFKAVVTM QVYRPTNMRA WSNMGISTSN QLGDRTLDVF HPTPKVSTYL
LALIISEFTS RSTPAGDAKP HSIIARPEMY DLSVYAFDVG RQILDRLGEA LAYPYYEFMP
KMDQAAIPDF SAGAMENLGL LTYRETNLLY SPIKTLTMTK QRIAAVIAHE QAHMWFGDLV
TCDWWSYTWL NEGFARYYQY HGTALVETDL ALGHQFVVEQ LQGVFQMDSS NSTHPMTDPT
VNSPSEVSGI FDNISYNKGA TFIRMIDYHL GGDRLINALR SYLRDREFST AVPNDLLRAL
QTQQQPQHEI DLVFNSWTTQ PGYPVVNVNI NSARSQATLT QKRFRSYSSE TSDTERWSIP
ITFASKTQYS LTDTTTRHVM HTQELNVTLT PAPNAWVIFN VQQVGYYRVN YDTDSWNIII
SALKETAHDG IHILNRAQIV DDLMNLARAG YVPYGTTFQM LEYLKSERNY IPWLSAFNGL
NHFRRRITDG NKELFGKYIR GLLDGVYTHL GFAPKTSEPT IDIYNRANVI SWACKYGHED
CLTNAKDQFA KLRNDPTNYI IPVDIRPTVY CEGLREGGQD AFNFLWQRYL SENVATEQII
ILNSLGCTNT DATVNALIDN ILSSAVRDQD KSSAFSNTYA HNEENIRRVW NYITNNHAKM
QTALGSYGSV ASYMSGVINR FRTNEELELV KTFINTHGNT FGDARESLNR AVANLEFDLY
WDSKYMDHVI KGIGGAGIRT ISAFLVLFTN GVEKRMVLTH FQTSYAKLFM PCFDQPDMKA
NYTLTVRRRA DMTAWSNMPI ATSAKDPNPD YILDTFHPTM SMSTYLLGLV VAEYSEKKIE
NTSGPEFFTI SHPSMIDYTE YVAQVGHRKL KVLEAFLDFP LSAFMTKIHL VAVPDFNAYA
MENPGLITFR ESLMLYNARK TSMLHKLRIA MVATHEIAHM WFGGVVTCEW WSYTWLNEGL
ATYFAHQTVP GVEESSILSH LFTINVLQCA LRNDADDSTI PMTNSDVETH EQIREMFYVV
SYEKSASVVR MMEHYMGRGD FQKSLMQYID KRKFNTATPD DLFAAFNNTL NHNEEFRDIF
YTYTRQPGYP VVIINVNEAR TSAEISQNKF HSYRKSIAGE DIWVIPITYT TRDEKNFTNT
SRAFVLNCND LEIPIDLTPD KWIIFNVQQV GYYRVNYDTK SWELIIEALK LSNHDGIHVI
NRAQIVDDLL ALAQSDNVPY TTVFDMLQYL LDEQEYVPWR AALTHFEFIS KRIPNNHRKL
FNNYLKFLIG NTYERLGFLP KSPNDPPLEI LHRGLIASWA CRVAHKPCLD EARKQFMEFR
KDTTAEINVD IRNVAYCEGV RDGDESTFEW MLQRYSEENM EIEQMTLLEG LGCANSESIV
KLYLNRIFSN DEIIRKNQKF HAFSHLLSYN PDNVNRVWDY VKNNHERMSK ISTFEINVDI
RNVAYCEGVR DGDESTFEWM LQRYSKENME IEQMTLLEGL GCANSESIVK LYLNRIFSND
EIIRKNQKFH AFSHLLSYNP DNVNRVWDYV KSNHERMSKI LTNGYKDVLK YVKCITMRMN
TPQQHEDLQK FIASNGHKFG QYRTGLEVAE KELGELMTWD SVHVTYENPR FPAASKCRQE
NLLLAGNTCP LEAFPCKIPN PLIPIPNGSA VDETFEIWRH RIVHIGIRFM NPHIELLHTP
INAVTVAKMA GKSEDVHAFV HREHGAIFHI LKSHLVVNFI KEHRLNEGQT IDGRLPGHVV
CLMMKVSRDF EGSHIAEIPT TRQIESIVNE LRTI
//
