ID   PLS2_BOVIN              Reviewed;         293 AA.
AC   Q3ZBG9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phospholipid scramblase 2;
DE            Short=PL scramblase 2;
DE   AltName: Full=Ca(2+)-dependent phospholipid scramblase 2;
GN   Name=PLSCR2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May mediate accelerated ATP-independent bidirectional
CC       transbilayer migration of phospholipids upon binding calcium ions that
CC       results in a loss of phospholipid asymmetry in the plasma membrane. May
CC       play a central role in the initiation of fibrin clot formation, in the
CC       activation of mast cells and in the recognition of apoptotic and
CC       injured cells by the reticuloendothelial system (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal proline-rich domain (PRD) is required for
CC       phospholipid scramblase activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phospholipid scramblase family.
CC       {ECO:0000305}.
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DR   EMBL; BC103299; AAI03300.1; -; mRNA.
DR   RefSeq; NP_001029608.1; NM_001034436.1.
DR   AlphaFoldDB; Q3ZBG9; -.
DR   STRING; 9913.ENSBTAP00000029993; -.
DR   PaxDb; Q3ZBG9; -.
DR   PRIDE; Q3ZBG9; -.
DR   Ensembl; ENSBTAT00000030005; ENSBTAP00000029993; ENSBTAG00000022227.
DR   GeneID; 513193; -.
DR   KEGG; bta:513193; -.
DR   CTD; 57047; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022227; -.
DR   eggNOG; KOG0621; Eukaryota.
DR   GeneTree; ENSGT00940000154435; -.
DR   HOGENOM; CLU_053024_2_0_1; -.
DR   InParanoid; Q3ZBG9; -.
DR   OMA; QNWHLWR; -.
DR   OrthoDB; 1015148at2759; -.
DR   TreeFam; TF314939; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000022227; Expressed in monocyte and 107 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017128; F:phospholipid scramblase activity; IBA:GO_Central.
DR   GO; GO:0017121; P:plasma membrane phospholipid scrambling; IBA:GO_Central.
DR   InterPro; IPR005552; Scramblase.
DR   PANTHER; PTHR23248; PTHR23248; 1.
DR   Pfam; PF03803; Scramblase; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..293
FT                   /note="Phospholipid scramblase 2"
FT                   /id="PRO_0000254023"
FT   TOPO_DOM        1..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..293
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..66
FT                   /note="Proline-rich domain (PRD)"
FT                   /evidence="ECO:0000250"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         143
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000250"
FT   LIPID           166
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O15162"
FT   LIPID           167
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O15162"
FT   LIPID           170
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O15162"
FT   LIPID           171
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O15162"
SQ   SEQUENCE   293 AA;  32577 MW;  07F0211003C01F7E CRC64;
     MDKQNVQMNP PHPGTNLTGP PGHIGYPGPQ AGYAVPPPGY ASPGPVGFPV QHQPVTGHPG
     APTQVPWMPA PLPPLNCPPG LEYLTQIDQL LIHQQIELLE VLIGFETNNK YEIKNSLGQR
     IYFAAEDTDC CTRNCCGPSR PFTMRILDNM GREVITLERP LRCTSCCFPC CLQEIEIQAP
     PGVPVGYVTQ TWHPCLPKFT IQNERREDVL RISGPCVICS CCADIDFEVK SLDDKYVVGK
     ISKHWTGLIK ELFTDVDNFG IQFPLDLDVK MKAVMLGACF LIDFMFFEMT RGE