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ACE3_MOUSE
ID   ACE3_MOUSE              Reviewed;         737 AA.
AC   D0G895;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Angiotensin-converting enzyme-like protein Ace3 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Ace3 {ECO:0000312|MGI:MGI:3644400};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:BAI48788.1};
RN   [1] {ECO:0000312|EMBL:BAI48788.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH IZUMO1, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION
RP   PHENOTYPE.
RC   TISSUE=Testis {ECO:0000312|EMBL:BAI48788.1};
RX   PubMed=20421979; DOI=10.1371/journal.pone.0010301;
RA   Inoue N., Kasahara T., Ikawa M., Okabe M.;
RT   "Identification and disruption of sperm-specific angiotensin converting
RT   enzyme-3 (ACE3) in mouse.";
RL   PLoS ONE 5:E10301-E10301(2010).
RN   [2] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=17597519; DOI=10.1186/1471-2164-8-194;
RA   Rella M., Elliot J.L., Revett T.J., Lanfear J., Phelan A., Jackson R.M.,
RA   Turner A.J., Hooper N.M.;
RT   "Identification and characterisation of the angiotensin converting enzyme-3
RT   (ACE3) gene: a novel mammalian homologue of ACE.";
RL   BMC Genomics 8:194-194(2007).
CC   -!- SUBUNIT: Interacts with IZUMO1. {ECO:0000269|PubMed:20421979}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       membrane {ECO:0000269|PubMed:20421979}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Disappears from acrosome reacted sperm. Co-
CC       localizes with IZUMO1 at acrosomal cap area.
CC       {ECO:0000269|PubMed:20421979}.
CC   -!- TISSUE SPECIFICITY: Expressed in sperm and testis (at protein level)
CC       (PubMed:20421979). Expressed in heart and testis (PubMed:17597519). Not
CC       detected in kidney, lung, liver, brain, ovary, spleen and thymus
CC       (PubMed:17597519, PubMed:20421979). {ECO:0000269|PubMed:17597519,
CC       ECO:0000269|PubMed:20421979}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Sperm have normal
CC       fertilizing ability. {ECO:0000269|PubMed:20421979}.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Glu residue in position 378 necessary for
CC       the catalytic activity. {ECO:0000305}.
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DR   EMBL; AB531024; BAI48788.1; -; mRNA.
DR   EMBL; AL596331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS59570.1; -.
DR   RefSeq; NP_001094923.2; NM_001101453.2.
DR   AlphaFoldDB; D0G895; -.
DR   SMR; D0G895; -.
DR   STRING; 10090.ENSMUSP00000140827; -.
DR   MEROPS; M02.971; -.
DR   GlyGen; D0G895; 1 site.
DR   iPTMnet; D0G895; -.
DR   PhosphoSitePlus; D0G895; -.
DR   jPOST; D0G895; -.
DR   MaxQB; D0G895; -.
DR   PaxDb; D0G895; -.
DR   PeptideAtlas; D0G895; -.
DR   PRIDE; D0G895; -.
DR   ProteomicsDB; 285579; -.
DR   DNASU; 217246; -.
DR   Ensembl; ENSMUST00000190995; ENSMUSP00000140827; ENSMUSG00000101605.
DR   GeneID; 217246; -.
DR   KEGG; mmu:217246; -.
DR   UCSC; uc011ygg.2; mouse.
DR   CTD; 217246; -.
DR   MGI; MGI:3644400; Ace3.
DR   VEuPathDB; HostDB:ENSMUSG00000101605; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   GeneTree; ENSGT00940000163921; -.
DR   HOGENOM; CLU_014364_3_0_1; -.
DR   InParanoid; D0G895; -.
DR   OMA; REVECHT; -.
DR   OrthoDB; 422699at2759; -.
DR   PhylomeDB; D0G895; -.
DR   BioGRID-ORCS; 217246; 2 hits in 68 CRISPR screens.
DR   PRO; PR:D0G895; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; D0G895; protein.
DR   Bgee; ENSMUSG00000101605; Expressed in spermatid and 4 other tissues.
DR   GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IBA:GO_Central.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IBA:GO_Central.
DR   CDD; cd06461; M2_ACE; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..737
FT                   /note="Angiotensin-converting enzyme-like protein Ace3"
FT                   /id="PRO_5008952182"
FT   TOPO_DOM        24..639
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        640..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        661..700
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        722..737
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   737 AA;  85874 MW;  149363A9C6372A61 CRC64;
     MNLPWALLLV LLSHRQLLPW LRTVGETSLN DFYSEAQAKL FLQFYEQTAQ VVLNEFMEAT
     WNYVTNITKQ NQKNMLQKEA DRSQFMLYFS TRARMFRTDH FLNQDVKRML RKLQNIDKSA
     LPTEDLLEYN RLLTYMETAY NRAEVCLDEG PCLTLEPDLQ EIMATSRDQK ELLWAWQGWR
     DAVGRQLRPV FEDYVRLSNK AAQYNGYKDM GALWRSKYES DTLEEDLEQL YKELQPLYLN
     LHAYVRRSLY RYYGPELIDL RGPIPAHLLG NMWAQSWNNI LDLVLPYPTK APEDITAIMK
     IQHWRPEKMF EEANLFFTSM GMLPAPPAFW IKSMMEKPAD GREVECHTSS WNFYKFNDFR
     VKKCTEVTLE DLLSVFHQMG HIQYFLQYQN LSVIYQEGAS PAFEEAVGSV IALSVSSHKY
     LLARGLLSQP HQDSEEEVNF LLGIALEKIA FIPFSYLVDK FRWKIFDGTI SKITYNQEWW
     NFRLKYQGLC PPVPRSDDDF DPGAKFHIPA NVPYIRYFLG LILQFQLHEA LCEASGHVGP
     LHQCDNYNSK VAGKILGDLL KLGSSRPWRE VLQEVTGESN ISTKAFLTYF KPLMDWLVTE
     NVKQGDTLGW PDFSCSFEEK ITSKVSFLGT DTEPEQAYLG QWVLLSMSFF MLVLILALGF
     RLHYLEKQLL DEDTMILKTL PYSYFLGIAM EPHQAARKQW LLLGLCCILM LCCIGLLIRI
     VTQNTENTPW MKNEGQS
 
 
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