ID Q1LWJ7_DANRE Unreviewed; 946 AA.
AC Q1LWJ7; A0A8M1N9G7;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=anpeplb {ECO:0000313|ZFIN:ZDB-GENE-030131-4781};
GN Synonyms=anpepa {ECO:0000313|RefSeq:NP_001038326.1}, fd60b03
GN {ECO:0000313|RefSeq:NP_001038326.1}, si:ch211-200o3.4
GN {ECO:0000313|RefSeq:NP_001038326.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-4781}, wu:fd60b03
GN {ECO:0000313|RefSeq:NP_001038326.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000060195};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000060195, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000060195};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000060195}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000060195};
RG Ensembl;
RL Submitted (AUG-2013) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:NP_001038326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001038326.1};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [4] {ECO:0000313|RefSeq:NP_001038326.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001038326.1};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; BX548061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001038326.1; NM_001044861.1.
DR STRING; 7955.ENSDARP00000060195; -.
DR MEROPS; M01.016; -.
DR PaxDb; 7955-ENSDARP00000060195; -.
DR Ensembl; ENSDART00000060196; ENSDARP00000060195; ENSDARG00000041083.
DR Ensembl; ENSDART00000060196.8; ENSDARP00000060195.6; ENSDARG00000041083.8.
DR GeneID; 558452; -.
DR KEGG; dre:558452; -.
DR AGR; ZFIN:ZDB-GENE-030131-4781; -.
DR CTD; 558452; -.
DR ZFIN; ZDB-GENE-030131-4781; anpepa.
DR ZFIN; ZDB-GENE-030131-4781; anpeplb.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_2_0_1; -.
DR OMA; RFEINYQ; -.
DR OrthoDB; 3085317at2759; -.
DR PhylomeDB; Q1LWJ7; -.
DR TreeFam; TF300395; -.
DR Proteomes; UP000000437; Alternate scaffold 18.
DR Proteomes; UP000000437; Chromosome 18.
DR Bgee; ENSDARG00000041083; Expressed in intestine and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; -; 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:SF172; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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|RuleBase:RU364040,
KW ECO:0000313|RefSeq:NP_001038326.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000000437};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 70..272
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 310..528
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 601..924
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 469
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 946 AA; 108519 MW; 82A6CB2615DFD397 CRC64;
MAKSTGMSKA LAIGIGVITV CSVGCLVVMA VFFQIQVGNN KPTPPPRPIL PTPLPTDLPE
SLRLPDSLIP ESYNVFLQPY LYAAITNNYT EQSYLFTGNS TVRVNCTKTS SRVFLHVHNI
NVTAVEVRKS DTNEKLPLKG YQIFKNETNF LDIHLEVAIK ENGTYDIFTE FEGELLEDLT
GFYASRYTGK GTDDEDEERF LATSLLQPTD ARTVFPCFDE PAMKAVFTIT IIHRPEIRAR
SNEDGDPRTI QINGTDWIRT TFKPTKKMSS YLLGFIIYDT HTFSYVSKGT RTKIHVHGRS
EAIDAGHADY ALETTETILS HYENIFGLRY PMSKIDQIAL PDFGVRAMEN WGFISYQESG
LLYDKETAST FDEEQVTTLI AHELAHQWFG NLVTMSWWND LWLKEGFATY MSYKGVEAVG
WDLKDLIVLR EIQTAFQMDS LNTSHPLSMN AYDVQTSSQI SELFDDITYS KGAAVLRMLA
TRMGENEFMK GVKMYLSKFQ FENTVPKDLW ECLNMDTHIK VDEFMKTWTE EVGYPVLTII
TDTGDTSQEQ FLLKKEGGHD SLWHIPIKYM TLKAGVKEFP NFFTDKGPDP IPDFKIGKDN
WLLANINCTG FYRVNYDEEN WNRLTAQLQK NHRIIPLINR GQLIDDAFNL ARAHRLNVTI
ALNLTKYLIN DLEYIPWESA LKNLDFFTLM FDRSEVYGPI MKYLRNLVTP LYEEYEEYTI
NGTIPIEKYT DQCNQVNAIT VACSNGLPEC ITMAKDLFSD YKNGSNPIHP NLRRAVYCSA
VASGDEDDWE YVWEEYQKAT VAAEKDKLRY ALSCTKEIWL LNRYLQYTLE PSKIRKMDMV
STISYIAQNV AGQPLAWDFI RGHWSYITQE YGAGIISLGS LLDVVTKRFS TEVELEELKQ
LQREQIQDDK WIAARALEQV IERTAANIIW VKENKQVVKD WFIAEL
//
