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EST5A_FELCA
ID   EST5A_FELCA             Reviewed;         545 AA.
AC   Q8I034;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Carboxylesterase 5A;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylesterase-like urinary excreted protein;
DE            Short=Cauxin;
DE   Flags: Precursor;
GN   Name=CES5A; Synonyms=CES7;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-57; 93-114; 151-172;
RP   248-264; 280-297; 308-330 AND 533-541, BIOPHYSICOCHEMICAL PROPERTIES,
RP   GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=12401131; DOI=10.1042/bj20021446;
RA   Miyazaki M., Kamiie K., Soeta S., Taira H., Yamashita T.;
RT   "Molecular cloning and characterization of a novel carboxylesterase-like
RT   protein that is physiologically present at high concentrations in the urine
RT   of domestic cats (Felis catus).";
RL   Biochem. J. 370:101-110(2003).
RN   [2]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=17045831; DOI=10.1016/j.cbpb.2006.05.015;
RA   Miyazaki M., Yamashita T., Hosokawa M., Taira H., Suzuki A.;
RT   "Species-, sex-, and age-dependent urinary excretion of cauxin, a mammalian
RT   carboxylesterase.";
RL   Comp. Biochem. Physiol. 145B:270-277(2006).
RN   [3]
RP   FUNCTION.
RX   PubMed=17052611; DOI=10.1016/j.chembiol.2006.08.013;
RA   Miyazaki M., Yamashita T., Suzuki Y., Saito Y., Soeta S., Taira H.,
RA   Suzuki A.;
RT   "A major urinary protein of the domestic cat regulates the production of
RT   felinine, a putative pheromone precursor.";
RL   Chem. Biol. 13:1071-1079(2006).
RN   [4]
RP   GLYCOSYLATION AT ASN-86.
RX   PubMed=17341822; DOI=10.1271/bbb.60599;
RA   Suzuki Y., Miyazaki M., Ito E., Suzuki M., Yamashita T., Taira H.,
RA   Suzuki A.;
RT   "Structural characterization of N-glycans of cauxin by MALDI-TOF mass
RT   spectrometry and nano LC-ESI-mass spectrometry.";
RL   Biosci. Biotechnol. Biochem. 71:811-816(2007).
RN   [5]
RP   INDUCTION.
RX   PubMed=16919690; DOI=10.1016/j.rvsc.2006.06.009;
RA   Miyazaki M., Soeta S., Yamagishi N., Taira H., Suzuki A., Yamashita T.;
RT   "Tubulointerstitial nephritis causes decreased renal expression and urinary
RT   excretion of cauxin, a major urinary protein of the domestic cat.";
RL   Res. Vet. Sci. 82:76-79(2007).
CC   -!- FUNCTION: Carboxylesterase present at high level in urine that
CC       regulates production of felinine, a probable pheromone precursor.
CC       Probably acts by hydrolyzing the peptide bond of the felinine precursor
CC       3-methylbutanol cyteinylglycine, producing felinine and glycine in cat
CC       urine. {ECO:0000269|PubMed:17052611}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=506 uM for p-NPA {ECO:0000269|PubMed:12401131};
CC         Vmax=7.61 umol/min/mg enzyme with p-NPA as substrate
CC         {ECO:0000269|PubMed:12401131};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Present at high level in urine. Expressed in the
CC       kidney proximal straight tubular cells and is secreted from the apical
CC       compartment of the cells into the urine (at protein level). In mature
CC       cats, it is present at higher level in intact males than in castrated
CC       males or in intact or spayed females. {ECO:0000269|PubMed:12401131,
CC       ECO:0000269|PubMed:17045831}.
CC   -!- DEVELOPMENTAL STAGE: Present in cats older than about 3 months, and its
CC       level increases with age. {ECO:0000269|PubMed:17045831}.
CC   -!- INDUCTION: Strongly down-regulated in cats suffering from
CC       tubulointerstitial nephritis (TIN). Excretion decreases immediately
CC       after castration. {ECO:0000269|PubMed:16919690,
CC       ECO:0000269|PubMed:17045831}.
CC   -!- PTM: N-glycosylated; contains a fucosylated complex carbohydrate.
CC       {ECO:0000269|PubMed:12401131, ECO:0000269|PubMed:17341822}.
CC   -!- MISCELLANEOUS: Protein specifically present in urine of cat. Present at
CC       high level in urine of members of the genus Felis and Lynx but not in
CC       urine of other felines.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AB045377; BAC22577.1; -; mRNA.
DR   RefSeq; NP_001009188.1; NM_001009188.1.
DR   AlphaFoldDB; Q8I034; -.
DR   SMR; Q8I034; -.
DR   STRING; 9685.ENSFCAP00000013286; -.
DR   ESTHER; felca-CAUXIN; Carb_B_Chordata.
DR   iPTMnet; Q8I034; -.
DR   PRIDE; Q8I034; -.
DR   GeneID; 445455; -.
DR   KEGG; fca:445455; -.
DR   CTD; 221223; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   InParanoid; Q8I034; -.
DR   OrthoDB; 754103at2759; -.
DR   BioCyc; MetaCyc:MON-20541; -.
DR   SABIO-RK; Q8I034; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:12401131"
FT   CHAIN           29..545
FT                   /note="Carboxylesterase 5A"
FT                   /id="PRO_0000308590"
FT   ACT_SITE        226
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        454
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17341822"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        281..292
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  60506 MW;  9F73FA693D271FA9 CRC64;
     MSGMWVHPGR TLIWALWVLA AVIKGPAADA PVRSTRLGWV RGKQTTVLGS TVPVNMFLGI
     PYAAPPLGPL RFKQPKPALP GNDFRNATSY PKLCFQDLEW LVSYQHVLKV RYPKLEASED
     CLYLNIYAPA HADNGSNLPV MVWFPGGAFK MGSASSFDGS ALAAYEDVLI VTTQYRLGIF
     GFFDTGDEHA RGNWALLDQV AALTWVRDNI EFFGGDPRSV TIFGESAGAI SVSSLILSPI
     ANGLFHKAIM ESGVAILPLL MRPPGDERKK DLQVLARICG CHASDSAALL QCLRAKPSEE
     LMDISKKLTF SIPVIDDFFF PDEPVALLTQ KAFNSVPSII GVNNHECAFL LSTEFSEILG
     GSNRSLALYL VHTFLNIPTQ YLHLVADHYF YNKHSPVEIR DSFLDLLGDV LFVVPGVVTA
     RYHRDAGAPV YFYEFQHPPQ CLNDTRPAFV KADHSDEIRF VFGGAFLKGD IVMFEGATEE
     EKLLSRKMMR YWANFARTGD PNGEGVPLWP AYTQSEQYLK LDLSVSVGQK LKEQEVEFWM
     NTIVP
 
 
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