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Database: UniProt
Entry: A0A3P8WD91_CYNSE
LinkDB: A0A3P8WD91_CYNSE
Original site: A0A3P8WD91_CYNSE 
ID   A0A3P8WD91_CYNSE        Unreviewed;       938 AA.
AC   A0A3P8WD91;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000024407.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000024407.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000024407.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   RefSeq; XP_008335053.1; XM_008336831.2.
DR   AlphaFoldDB; A0A3P8WD91; -.
DR   STRING; 244447.ENSCSEP00000024407; -.
DR   Ensembl; ENSCSET00000024737.1; ENSCSEP00000024407.1; ENSCSEG00000015587.1.
DR   GeneID; 103398274; -.
DR   KEGG; csem:103398274; -.
DR   CTD; 64167; -.
DR   GeneTree; ENSGT00940000162653; -.
DR   InParanoid; A0A3P8WD91; -.
DR   OMA; NVWMNMS; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000265120; Chromosome Z.
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:SF239; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 2; 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   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:UP000265120};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..938
FT                   /note="Aminopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018111730"
FT   DOMAIN          54..240
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          275..481
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          597..916
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         347
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            432
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   938 AA;  107632 MW;  0D8EA9D87D804294 CRC64;
     MASVRLLLLF LFNLPLAECW SSPGSTNTLG EPSVDTHNLS FPWSRLRLPR YVIPLHYRLL
     LHPNLTSLSF TGSVQIQIAV QNNTNWIVLH SKGLQISRAT ILDQNLSPLS DQVLPVLYKP
     SHEQIGIFSP RVLSTGPTYF LYIEFGADIA EGFSGFYRST YRTTAGKTRT LASTHFEPTD
     ARTAFPCFDE PNFKANFSVR IRRSPAHIAL SNMPVDRTVK VNSELLEDRF AVSVKMSTYL
     VAFVICDFRS ISATTSTGVK VSIYAAPEKW PQTHYALDVA VKMLDFYEKY FNIRYPLPKQ
     DLIAIPDFQS GAMENWGLTT YRETSLLFDP LTSSLHDKLW VTMVIGHELA HQWFGNLVTM
     VWWNDIWLNE GFARYMEYIS VEGTYPELAV EEYLLHTCFA AVGLDSLNSS RPISNAAESP
     TQIEEMFDTV SYDKGACVLH MLRYFLTDDV FQSGIVRYLR KYSYKNAQNQ DLWDSLSNTC
     TEDDFVSGKH CYTSEHATRN AYMFAGEHLN LTAMMNTWTL QKGVPLVTVT RRGPRLLIRQ
     NRFLRTVMPS DPLWPSLQKG FLWHIPLTYK TNGSSLIHRH LMTTHTDSIH VGEEVSWVKV
     NTDMTGYYLV HYEDGGWDNM IDLLRENHTA LSYKDRTHLI HNAFQLVTAG HLPIHKALDL
     ISYLQKETNT VPLLEGLGYL DAFYHLIEKR NEPELTHILG SYILRFFREV INQQTWSDEG
     TVSQRRLRSE VLSLACHLSD PSCIQQAKSI FKDWLHSNGT LNLPTDVAQT VYSVGAQDDH
     GWKTLLHTYN FSLSEVLKDK ILHALSRSTD ISKLERLLQL GLEGNVIRMQ DLSHVVLMVA
     RNPQGHHLSW NFVKKNWDML VKKFHLGSFS IRNILIGTTS QFSTQEELND VQRFFESIKE
     QASELRATQV ALDNVQKNVR WIQRNLETLR KWLSDRVK
//
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