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Database: UniProt
Entry: A0A498MCD5_LABRO
LinkDB: A0A498MCD5_LABRO
Original site: A0A498MCD5_LABRO 
ID   A0A498MCD5_LABRO        Unreviewed;      1599 AA.
AC   A0A498MCD5;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Hepatic triacylglycerol lipase-like protein {ECO:0000313|EMBL:RXN17483.1};
GN   ORFNames=ROHU_037000 {ECO:0000313|EMBL:RXN17483.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN17483.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN17483.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN17483.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN17483.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000256|ARBA:ARBA00006175}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXN17483.1}.
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DR   EMBL; QBIY01012744; RXN17483.1; -; Genomic_DNA.
DR   STRING; 84645.A0A498MCD5; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00333; MIP; 1.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   CDD; cd00176; SPEC; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 2.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR002333; Lipase_hep.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR46349; CINGULIN-LIKE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46349:SF6; MYOSIN_TAIL_1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF00230; MIP; 2.
DR   PRINTS; PR00824; HEPLIPASE.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF81338; Aquaporin-like; 2.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   PROSITE; PS00221; MIP; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        962..985
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        991..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1016..1039
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1054..1075
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1142..1453
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1108..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1599 AA;  179640 MW;  42ABF0AF8E5C592B CRC64;
     MESFGAQDGR SQSDPVRASQ DDSGSFGVQV QVQGISGRPY VVLNAQGRRV PRSPEYPDVF
     LAEHRRQEFV SNMSGGASST QTPRPDHHRS LRVFKNPSVQ LLNYQRNPEI LKPYDPRNSR
     GWCSSPSSPV MVKRARIPVP GAGRDRVQEP AVESVPCQPS HIICRMSVPA SETYDTGTAS
     AGSPRTGRVG HRGRIAPEEK RRSRSLESRS DGIRTEVGGF AQSGQGERSE VNEENGSGQA
     TPDLLKGRRE LPDQPDEETA KLVMVNYLKD GSCEGEAVIR QRVELMFDKI HMLKFRALEE
     FAFAAPLEEV NDLKDRRAAL ERHVSLLQQQ LQEAKQDSDG LSEEKEETNA ELKRLQEALE
     RSEQEQITLR HKLTDMEKEL QTSLDQLLQA RRARDQCRSD MRDLQQQLSD IHDELDSAKS
     CEAGERDRLL QDLSELRGEF EALQRVQEEQ EEALHRRDRE LTALRGALEE EISAHARDVE
     ALQEEHQQEI HRLLEATQEA KEAPDSTRLR PPPLLQSVAL LGQKVLEVAA EKGAGQTLIA
     ELKQTKAELQ LKISALEEQI SSLDHLIQQK QEQEKLLTER VEQLTMEKRN LEEELQEVRQ
     QEDDMCGANR ALMRHLEDTQ GELSRLTRAH RELKERFEEE RRRTEELQRR RSELEEERRS
     QDRVLERLHD EMSAAVTGSE QETQRLQEEN KDLRGRVSQL EGSQRLGQDA VVSELQLHVQ
     ELEERLLGEE KEKSDLQQLN RRLERRMKEL TLHLEEEKLS LQDQRDQRQL DEAEEEIERL
     ENSRKKLQRD VEEQQEISDQ LKTEICGLRN HISPVRRTRS IMKHHCALKH GIFKEFLAEF
     LGTFVLVLFG CGSVAQTVLS RNTLGEPLTV HIGFSTGLMM GVYVAGGVSG NTHTHTHTHT
     GYISITHRNS SALTREPEPQ ASDHCLSQNR SINRIHSSFC GHLNPAVSLA MVILGKLKIW
     KFPIYVAAQM LGAFVGAAAV FGLYYDAFMD FTSGILSVTG INATGHIFAS YPGRHLTVLG
     GFVDQVVGTG MLVLCILAVV DGRNIGAPHG VEPLAVGLIL LGISVSMGLN CGYPLNPARD
     LGPRLFTAAA GWGMEVFRLS FSGSRADADP QEKLLTPPDD HESPERFTPH DCRHSASETH
     SAPPVKTVLK SSFHLYHEGS VFEETCAVVP FRSETLHSCA YNHGDPLVMI IHGWKINGLM
     ETWIFDLASA LKVRLGRVNV FISDWRSLAR QPYPIAAKNS RQVGQDVATL LKWLEEVAQL
     SMDDVHLIGY SLGAHVAGFA GSHFRGLRKV GRITGLDPAA PHFEGLPAFD RLSPDDAQFV
     DAIHTFTGNS FMPGVGIKQS VAHVDFYPNG GSFQPGCKML DIYSNVFQYG LEGVPKTIKC
     AHERAVKLFT DSLVNASQPI IGYRCRDDST FNKGLCLDCK QMRCNTLGFD VRRERVGRNA
     KGLYLRTGPQ VPYRVFHYQI RVLLKNLIEP VEASLSVTLN GTGGESPELP IILHQESTGL
     KSFSSLLAVA SDLGQLSSVR LVWKGELVWS NWMRRVRNIM NWNTSDQDTE LSVWRICIKS
     GESQEKMWFC GASAGVSRLR ISEEQEFRRC QSSSSPSQT
//
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