ID   K9IM67_DESRO            Unreviewed;       654 AA.
AC   K9IM67;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA48628.1};
RN   [1] {ECO:0000313|EMBL:JAA48628.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA48628.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative phospholipase. {ECO:0000256|RuleBase:RU364138}.
CC   -!- SIMILARITY: Belongs to the phospholipase B-like family.
CC       {ECO:0000256|ARBA:ARBA00007835, ECO:0000256|RuleBase:RU364138}.
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DR   EMBL; GABZ01004897; JAA48628.1; -; mRNA.
DR   AlphaFoldDB; K9IM67; -.
DR   GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.60.20; -; 1.
DR   Gene3D; 2.10.70.60; Phospholipase B-like, domain 1; 1.
DR   Gene3D; 1.10.439.20; Phospholipase B-like, domain 2; 1.
DR   InterPro; IPR007000; PLipase_B-like.
DR   InterPro; IPR043040; PLipase_B-like_dom1.
DR   InterPro; IPR043041; PLipase_B-like_dom2.
DR   InterPro; IPR043042; PLipase_B-like_dom3.
DR   PANTHER; PTHR12370:SF3; PHOSPHOLIPASE B-LIKE 2-RELATED; 1.
DR   PANTHER; PTHR12370; PHOSPHOLIPASE B-RELATED; 1.
DR   Pfam; PF04916; Phospholip_B; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364138};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU364138};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU364138}; Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   654 AA;  72419 MW;  EFA15B8488D44D71 CRC64;
     MVAPRCVTPG ARLVLALTRA LALLVGLFLS GLTGAIPTPK GSWGPGGLDP PPSRSRSVLL
     DAGTGQLRLV DGRHPDAVAW ANLTNAIRET GWAFLELHTD GHYNDSLQAY AAGVVEAAVS
     EELIYMHWMN TVVNYCGPFE YEVGYCERLK SFLEANLEWL QGEMELNKDS AYWHQVRLTL
     LQLKGLEDSY EGSVTFPTGK FTIKPLGFLL LQISGDLEDL ELALNKTKTR HTVGSGSCSA
     LIKLLPGHSD LLVAHNTWNS YQNMLRIVKK YWFQFREGPQ EDSPLASGNK LVFSSYPGTV
     FSCDDFYVLG SGLVTLETTI GNRNPALWKY VTPRDCVMEW VRNIVANRLA VDGDTWAGVF
     KRFNSGTYNN QWMIVDYKAF VPGGPSPGSR VLTVLEQIPG MVVVADRTSE LYQKTYWASY
     NIPSFETVFN ASGLQALVAQ YGDWFSYDRS PRAQIFQRNQ SLVHDMASMI QLMRYNDFLH
     DPLSLCKACD PQPNGENAIS ARSDLNPANG SYPFQALQQR SHGGIDVKVT SRALAKALRL
     VAASGPTWDQ VPPFQWSTSP FSSLLHMGQP DLWKFSPIES RDLDLPGSLS SGNLPWVGHR
     TCRGPELTPS LPRWVSVFCL PLLHCVSLSF SFCFSVLSAS LSPPPWGPIL RLPP
//