ID   TALLP_MESAU             Reviewed;         398 AA.
AC   Q3YBN2;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Tear acid lipase-like protein {ECO:0000303|PubMed:17141562};
DE            Short=TALLP {ECO:0000303|PubMed:17141562};
DE   Flags: Precursor;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000312|EMBL:AAZ73232.1};
RN   [1] {ECO:0000312|EMBL:AAZ73232.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-37; 330-339; 364-376 AND
RP   377-387, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, INDUCTION, AND GLYCOSYLATION.
RC   TISSUE=Lacrimal gland {ECO:0000303|PubMed:17141562};
RX   PubMed=17141562; DOI=10.1016/j.bbalip.2006.10.002;
RA   Paliwal A., De P.K.;
RT   "Purification, cloning and regulation of a novel acid-lipase-like protein
RT   of hamster expressed in lacrimal glands and tears during lactation.";
RL   Biochim. Biophys. Acta 1771:55-65(2007).
CC   -!- FUNCTION: Female-specific protein which lacks detectable lipase
CC       activity against a range of substrates. Binds the hydrophobic lipid 1-
CC       aminoanthracene with high affinity. {ECO:0000269|PubMed:17141562}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17141562}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17141562}.
CC       Note=Secreted by the female lacrimal gland into tears.
CC       {ECO:0000269|PubMed:17141562}.
CC   -!- TISSUE SPECIFICITY: Expressed in female lacrimal gland acinar cells
CC       from where it is secreted into tears (at protein level).
CC       {ECO:0000269|PubMed:17141562}.
CC   -!- DEVELOPMENTAL STAGE: Expressed primarily during lactation although very
CC       low levels are detected in a small percentage of non-lactating females
CC       (at protein level). Not expressed in late-pregnant or 1-day postpartum
CC       dams but high levels are found in 9-day and 20-day postpartum lactating
CC       dams with no expression 20 days after weaning (at protein level).
CC       {ECO:0000269|PubMed:17141562}.
CC   -!- INDUCTION: Repressed by the androgen dihydrotesterone (DHT), the
CC       estrogen estradiol (E2) and the thyroid hormone triiodothyronine (T3)
CC       (at protein level). {ECO:0000269|PubMed:17141562}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17141562}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000255|PIRNR:PIRNR000862}.
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DR   EMBL; DQ144735; AAZ73232.1; -; mRNA.
DR   RefSeq; NP_001268622.1; NM_001281693.1.
DR   AlphaFoldDB; Q3YBN2; -.
DR   SMR; Q3YBN2; -.
DR   STRING; 10036.XP_005063743.1; -.
DR   ESTHER; mesau-q3ybn2; Acidic_Lipase.
DR   GeneID; 101824484; -.
DR   eggNOG; KOG2624; Eukaryota.
DR   OrthoDB; 651396at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR006693; AB_hydrolase_lipase.
DR   InterPro; IPR025483; Lipase_euk.
DR   Pfam; PF04083; Abhydro_lipase; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:17141562"
FT   CHAIN           20..398
FT                   /note="Tear acid lipase-like protein"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433366"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P07098"
FT   ACT_SITE        340
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P07098"
FT   ACT_SITE        369
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P07098"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        243..252
FT                   /evidence="ECO:0000250|UniProtKB:P07098"
FT   CONFLICT        369
FT                   /note="H -> E (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   398 AA;  44666 MW;  E5B1E10EB2FFD030 CRC64;
     MSWLLSTMCL VHVCGNIFCL FETTTNPEAY MKVSKIVNHW GYTSEEYEAV TEDGYILPLN
     RIPHGKNNIN STAPKKVVLC QHGLFSTAGV WVSNPPSNSL AFILADAGFD VWMGNSRGST
     WAKKHLYLDP NSKEFWAFSF DEMIKYDLPA TINFILKKTG QKQIYYIGHS QGALIALGAF
     STNQKLAEKI KLCFLLAPIA TLKHVEGIVS LLPYFYPTAF KVVFSEKEFL SAVAFSKLHG
     YSCNAKVIND GCVAIFLSMT GYVPQHLNKS RVDVYIRHSL AGTSVQTLLH YRQAIKKGVF
     EAYDWGSQSL NMLHYNQTTP PLYNVEDMKI PTAMWSGGKD SLADTKDVAH LVPKISNLIY
     HKITADFSHL DFTVGKNAYY VSNDILKLLD KSETENLH