ID E9HM96_DAPPU Unreviewed; 1130 AA.
AC E9HM96;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Aminopeptidase N {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAPPUDRAFT_203797 {ECO:0000313|EMBL:EFX67143.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX67143.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX67143.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
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; GL732685; EFX67143.1; -; Genomic_DNA.
DR AlphaFoldDB; E9HM96; -.
DR STRING; 6669.E9HM96; -.
DR MEROPS; M01.A09; -.
DR EnsemblMetazoa; EFX67143; EFX67143; DAPPUDRAFT_203797.
DR KEGG; dpx:DAPPUDRAFT_203797; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_2_2_1; -.
DR InParanoid; E9HM96; -.
DR OMA; IWARANA; -.
DR PhylomeDB; E9HM96; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 2.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; 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:SF276; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 2.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 2..224
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 326..520
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 556..780
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 864..1130
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 242..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 629
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 628
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 714
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1130 AA; 127578 MW; 258B059425549670 CRC64;
MFYKESQYAD WKIYMTSLVK PYYDFVGFQE TESDAHLTIL SRNDALNWAC KLKIADCVAN
VQSQYAALMQ EPDMRLSPNQ RNFILCAGVE NGRQPEWNFA YDQYRSTDNG NFLVAMTCTR
ESSIIYDLLS KMLDPNSIRS EDVDTLFGNL AANPIGNTMA LDFLTRRWND IEKALGTSHF
VYFFRSLCDR LNTPAQYDQM IKLRDDHIDI LNSITVEQGL DIVRANVEWM TLNQEEIGGW
LKNPSTATAL PTTEPTTETT TEIDVTSTVE PGTEDTTTST ASSTASSTTT PAPTTTTPAP
TPTPTPTTTT APSSGEDMRL PGDIIPITYN IRMLPFVELI ASGNFTTDGY VEIVAECIRA
TSNISINSAD LDIKIGTISI LDMESNSPIA MVNFIDEQSS REIVTIQTAV PLAVGKRYKI
SMSFLSTLNN ELRGFYRSSY VEEGERKWLA VTQFESTDAR RAFPCFDEPS MKANFTVTLG
RKDTMTSVSN MPQTKSGPIA GMTGYVWDYF APSVKMSSYL VAFLVSDFIN IPAKPGVSNV
QFRIWARANA ANITSYAIDI GPRILEYYES YFSIDYPLAK QDMAAIPDFA AGAMENWGLI
TYREQDLLID TETASARQKQ RVAIVMAHEL AHQWFGDLVT MEWWNAIWLN EGFASYMEFI
GTDSVEPDFK MNDQFVIENL QYVFGIDALE TSRPINIEVN TPEEISSLFD AISYEKGSCV
VRMCADMLGI ETFKRGLTRY LSTNAYGNAQ QDDLWQAMQE QADEEGIVLP ATVKEILDTW
TYKMGYPVIT VTRDYATGGA LVTQERFLLR KSNTSEVDPT VYQWWVPLTY INSKVNVAEK
LSEWMSKDEV SVSLSNLGAS ADQWVIFNVD QQNYYRVAYD KDNYRLITEQ LMDDHEQIVP
NNRAQLLDDT FILASVHTVP YKRALDLSLY LAQEKEYVPW NAVLAEFNYI DSMLHNQAQF
PDWTIHLTKL VTPYYEHVGF QESKTDAQLT LYARTDAMSW ACRLKIADCV DNSKAKYAEL
MNDPDNTTIL SANQKSVILK TGVENGGQSE YDFAFNQYTS KYDTSFLIAA TCSRDSSRLY
NLLEKMLDSE SGIRLGDVNT LFNNVASNPL GNLIATDFLV NRWNDIEKSW
//
