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Database: UniProt
Entry: S4RTN2_PETMA
LinkDB: S4RTN2_PETMA
Original site: S4RTN2_PETMA 
ID   S4RTN2_PETMA            Unreviewed;       527 AA.
AC   S4RTN2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Zgc:152830 {ECO:0000313|Ensembl:ENSPMAP00000008572.1};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000008572.1, ECO:0000313|Proteomes:UP000245300};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000008572.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   STRING; 7757.ENSPMAP00000008572; -.
DR   Ensembl; ENSPMAT00000008610.1; ENSPMAP00000008572.1; ENSPMAG00000007792.1.
DR   GeneTree; ENSGT00530000063255; -.
DR   HOGENOM; CLU_013734_0_1_1; -.
DR   OMA; ISCFKAP; -.
DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        97..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          356..363
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   527 AA;  57357 MW;  3113475C6C03EB8E CRC64;
     MEAVWALNIV HVTTIKDDRF DGVVVVTDNI TNLSGDLQGI QDKLAAYVKA DAAFYKEVSV
     VPCQCSMEKR LVFSPTGPLN RDYDDVRRFS DAAYSGILYI ALCCGFTDCF FLMLLLLTPI
     VSQQGPFNDA PLVGALGALH ALYVPIEVRE ALPEKKSKAE LLGLWVASDA EGQHLVKVVT
     ALVVYRDIGG SDPERMAAPK VAEYLETIFK DTTVLMKVIS DPDVFKKEFP CLAAVNRCAN
     XASHFPKRMC ESPLIVTSDL CVFVTLTLGA ILGVGAGICR DPGVFGKGHN TTKEWWPPNF
     SHNYIGVIYI ILAKLKPKNI RVVGVLAMVR NSVGSDCYVA DEIVTSRAGK RVRVGNTDAE
     GRMVMADLLC LLKEKAVSAV NPELYTIATL TGHAIRAVGP EYTLIMDNGP AREAGNCQEW
     FKVGERIGDP FELSTIRRED YVFHAGKSEY EDVLQCNNLP SSATPRGHQS PAAFLVLTSG
     MDAHGLDSEK PLRYSHVDIA GSSGPFPGTP TGAPIVAMAA HFLFKRL
//
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