ID A0A3B4HBM6_9CICH Unreviewed; 873 AA.
AC A0A3B4HBM6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=npepps {ECO:0000313|RefSeq:XP_005751739.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000031143.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000031143.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005751739.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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_005751739.1; XM_005751682.1.
DR AlphaFoldDB; A0A3B4HBM6; -.
DR STRING; 303518.ENSPNYP00000031143; -.
DR Ensembl; ENSPNYT00000031894.1; ENSPNYP00000031143.1; ENSPNYG00000023488.1.
DR GeneID; 102197922; -.
DR CTD; 9520; -.
DR GeneTree; ENSGT00940000155246; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; 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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_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:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000695023};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 16..201
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 236..453
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 534..847
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 394
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 873 AA; 98102 MW; 4ED8F9E94FDB1977 CRC64;
MPERRPFVRL PTDVYPVNYG LSLKPDLIDF TFEGKLEALV EVTQATNQIV MNCADIDIIT
ASFVPQGGEE INATGFNYQN EDEKVTLSFP SALQKGFGTL KIDFVGELND KMKGFYRSKY
TSPTGEIRYA AVTQFEATDA RRAFPCWDEP AIKATFDITL IVPKDRVALS NMNVIDRKPH
PDDENLVEVK FATTPIMSTY LVAFVIGEYD YVESQSSDGV MVRVYTPVGK AEQGKFALEV
ATKTLPFYND YFSVPYPLPK IDLIAIADFA AGAMENWGLV TYRETALLID PKNSCSSSRQ
WVALVVGHEL AHQWFGNLVT MEWWTHLWLN EGFASWIEYL CVDHCFPEYD IWTQFVSADY
TRALDLDALD SSHPIEVNVG HPSEVDEIFD AISYSKGASV IRMLHNYIGD EDFRKGMNAY
LLKFQHKNAS TEDLWDCLEQ ASGKPIAAVM GSWTKQMGFP IIAVDQEQQG DDCVLKISQK
KFCASGPHNE ENCPSWMVPI SICTSEDPKC TKLKVLLDRQ ETTITLNSVG PDQWIKINPG
TVGFYRIQYS SSMLESLLPG IRDLSLQPVD RLGLQNDLFS LSRAGMISTV EVLKLMEAFV
NEPNYTVWSD LSCNLGVLSS LLSHTDFHEE IQEFIRDLFT PIGLKLGWDS KPGEGHLDAL
LRSLVLGKLG KAGHKPTLEE ARRRFKDHVD GKQVLPADLR SPVYLTVLKH GDSATLDTML
KLHKQADMQE EKNRIERVLG AISAPDLIQK VLNFALSEDV RPQDTVSVIG GVAGSSKQGR
KAAWKFVKDN WEELYNRYQG GFLISRLIKL TVDGFAIDKM AVEVKSFFES HPAPAAERTV
QQCCENILLN AAWLKRDAED IHQYLLQRKA PPV
//
