ID C3ZRD4_BRAFL Unreviewed; 725 AA.
AC C3ZRD4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=BRAFLDRAFT_89426 {ECO:0000313|EMBL:EEN44873.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN44873.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN44873.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN44873.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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 EMBL; GG666665; EEN44873.1; -; Genomic_DNA.
DR RefSeq; XP_002588862.1; XM_002588816.1.
DR AlphaFoldDB; C3ZRD4; -.
DR STRING; 7739.C3ZRD4; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; C3ZRD4; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C: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; -; 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; 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; 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 Membrane {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 Transmembrane {ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 120..307
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 346..560
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
SQ SEQUENCE 725 AA; 82200 MW; FD188E0C7803C540 CRC64;
MEDGECDIAI IDGMPPSADG RATMDGTMNR VEQLQEEPCE RNDEDERIFV KKWQIACVLM
FVLVAVLAAV YFVVIRTKVN RSPHNFYTAR SSLEPFYPAP TFPTTEGPQE ITRLPEYLLP
YNYKVKLRLD LSETTFTGST TINLRCLQAT QVIVLDCIEG NITNASVSVV DLTTADVQVV
IELLYDDSEG RLVVYLGKRL QEGRIYKLEI AEFTGELRTQ PPGLYTTDYR HSDGLRQLLV
SSLKPMGARY VFPCMDDPAM KATFDVTIEH PKGQTALSNM PSKTKTVLTD GWVREEFYRT
PKMSTHLLGF ALFDGLTSLE AVISRGRVVR VWAPFDPEEN PSVEVALNTT IDAIHNIEQL
VPVEYQLTKT DVIPVPGLSV PSSDYCGLLM IRETALFCDG QESSMSQQLK CELAISKAVA
HNWFGNSVTV EWWDDLWLTE ALSTMLAYES VAYQRPDVNI CDLQWDEMIQ PAMAADIFSR
VDLSSYGHAA AIGEDPAVGG KGIGLLRMLD TIISDKEFLK AIENVLARFS HDNMNRSQFW
DAVSEATGFR IDVAAFMEPW VTQLGYPYVS IGRYQERDES RNQYFVQLPF YYSGFVSFMR
HLQTITIPPD IRESVIHVGI SAGDENVWWH VWKQSNASAI SAQDRQIFLC GLAASQQEWV
LWRLIFSLLE HFSSSVQEKY LRDLLDDAVH ATRLNQRYID RNMPYLQDWL KVPCATRVDT
RETNP
//
