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Carboxylesterase 5A (EC 3.1.1.1) (Carboxylesterase-like urinary excreted protein homolog) (Cauxin)

 EST5A_HUMAN             Reviewed;         575 AA.
Q6NT32; B7Z252; B7ZLB6; Q8NBC8; Q96DN9;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 117.
RecName: Full=Carboxylesterase 5A;
EC=3.1.1.1;
AltName: Full=Carboxylesterase-like urinary excreted protein homolog;
Short=Cauxin;
Flags: Precursor;
Name=CES5A; Synonyms=CES7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Liu Q., Hamil K.G., French F.S., Hall S.H., Zhang Y.-L.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND
VARIANT GLU-537.
TISSUE=Amygdala, and Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Involved in the detoxification of xenobiotics and in the
activation of ester and amide prodrugs. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a
carboxylate. {ECO:0000255|PROSITE-ProRule:PRU10039}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q6NT32-1; Sequence=Displayed;
Name=2;
IsoId=Q6NT32-2; Sequence=VSP_029006;
Name=3;
IsoId=Q6NT32-3; Sequence=VSP_029005;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q6NT32-4; Sequence=VSP_043296;
Note=No experimental confirmation available.;
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
-!- CAUTION: Was termed (Ref.1) CES5. {ECO:0000305}.
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EMBL; AY907669; AAX86044.1; -; mRNA.
EMBL; AK056109; BAB71094.1; -; mRNA.
EMBL; AK090997; BAC03565.1; -; mRNA.
EMBL; AK294334; BAH11738.1; -; mRNA.
EMBL; AC007335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC147362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069501; AAH69501.1; -; mRNA.
EMBL; BC069548; AAH69548.1; -; mRNA.
EMBL; BC117126; AAI17127.1; -; mRNA.
EMBL; BC143692; AAI43693.1; -; mRNA.
CCDS; CCDS10755.1; -. [Q6NT32-2]
CCDS; CCDS45490.1; -. [Q6NT32-1]
CCDS; CCDS54012.1; -. [Q6NT32-4]
RefSeq; NP_001137157.1; NM_001143685.1. [Q6NT32-1]
RefSeq; NP_001177087.1; NM_001190158.1. [Q6NT32-4]
RefSeq; NP_659461.1; NM_145024.2. [Q6NT32-2]
UniGene; Hs.350800; -.
ProteinModelPortal; Q6NT32; -.
SMR; Q6NT32; -.
STRING; 9606.ENSP00000428864; -.
ESTHER; human-CES5A; Carb_B_Chordata.
MEROPS; S09.960; -.
iPTMnet; Q6NT32; -.
PhosphoSitePlus; Q6NT32; -.
BioMuta; CES5A; -.
DMDM; 74758113; -.
PaxDb; Q6NT32; -.
PeptideAtlas; Q6NT32; -.
PRIDE; Q6NT32; -.
Ensembl; ENST00000290567; ENSP00000290567; ENSG00000159398. [Q6NT32-1]
Ensembl; ENST00000319165; ENSP00000324271; ENSG00000159398. [Q6NT32-2]
Ensembl; ENST00000518005; ENSP00000428571; ENSG00000159398. [Q6NT32-3]
Ensembl; ENST00000521992; ENSP00000428864; ENSG00000159398. [Q6NT32-4]
GeneID; 221223; -.
KEGG; hsa:221223; -.
UCSC; uc002eip.3; human. [Q6NT32-1]
CTD; 221223; -.
DisGeNET; 221223; -.
EuPathDB; HostDB:ENSG00000159398.15; -.
GeneCards; CES5A; -.
HGNC; HGNC:26459; CES5A.
HPA; HPA047635; -.
neXtProt; NX_Q6NT32; -.
OpenTargets; ENSG00000159398; -.
PharmGKB; PA142672130; -.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
GeneTree; ENSGT00760000118946; -.
HOGENOM; HOG000091866; -.
HOVERGEN; HBG008839; -.
InParanoid; Q6NT32; -.
KO; K15743; -.
OMA; LPLWPAY; -.
OrthoDB; EOG091G03ZC; -.
PhylomeDB; Q6NT32; -.
TreeFam; TF315470; -.
GenomeRNAi; 221223; -.
PRO; PR:Q6NT32; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000159398; -.
CleanEx; HS_CES7; -.
ExpressionAtlas; Q6NT32; baseline and differential.
Genevisible; Q6NT32; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
Pfam; PF00135; COesterase; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Polymorphism; Reference proteome; Secreted;
Serine esterase; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 575 Carboxylesterase 5A.
/FTId=PRO_0000308591.
ACT_SITE 226 226 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039}.
ACT_SITE 345 345 Charge relay system. {ECO:0000250}.
ACT_SITE 454 454 Charge relay system. {ECO:0000250}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 94 121 {ECO:0000250}.
VAR_SEQ 1 106 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_029005.
VAR_SEQ 1 24 MSGNWVHPGQILIWAIWVLAAPTK -> MAVLVCPASCHGL
KEFRIRRGMWRLCLVYYFYPASSTLYVLRIDVLNYTSKDE
(in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043296.
VAR_SEQ 425 474 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_029006.
VARIANT 71 71 R -> Q (in dbSNP:rs2397965).
/FTId=VAR_036836.
VARIANT 261 261 E -> K (in dbSNP:rs11076126).
/FTId=VAR_036837.
VARIANT 344 344 H -> Q (in dbSNP:rs11860946).
/FTId=VAR_036838.
VARIANT 499 499 G -> R (in dbSNP:rs16955812).
/FTId=VAR_036839.
VARIANT 537 537 D -> E (in dbSNP:rs11860456).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_036840.
CONFLICT 343 343 N -> S (in Ref. 2; BAC03565).
{ECO:0000305}.
SEQUENCE 575 AA; 63926 MW; 6F5B735BDEFC9C09 CRC64;
MSGNWVHPGQ ILIWAIWVLA APTKGPSAEG PQRNTRLGWI QGKQVTVLGS PVPVNVFLGV
PFAAPPLGSL RFTNPQPASP WDNLREATSY PNLCLQNSEW LLLDQHMLKV HYPKFGVSED
CLYLNIYAPA HADTGSKLPV LVWFPGGAFK TGSASIFDGS ALAAYEDVLV VVVQYRLGIF
GFFTTWDQHA PGNWAFKDQV AALSWVQKNI EFFGGDPSSV TIFGESAGAI SVSSLILSPM
AKGLFHKAIM ESGVAIIPYL EAHDYEKSED LQVVAHFCGN NASDSEALLR CLRTKPSKEL
LTLSQKTKSF TRVVDGAFFP NEPLDLLSQK AFKAIPSIIG VNNHECGFLL PMKEAPEILS
GSNKSLALHL IQNILHIPPQ YLHLVANEYF HDKHSLTEIR DSLLDLLGDV FFVVPALITA
RYHRDAGAPV YFYEFRHRPQ CFEDTKPAFV KADHADEVRF VFGGAFLKGD IVMFEGATEE
EKLLSRKMMK YWATFARTGN PNGNDLSLWP AYNLTEQYLQ LDLNMSLGQR LKEPRVDFWT
STIPLILSAS DMLHSPLSSL TFLSLLQPFF FFCAP


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