PEBP2_MOUSE
ID PEBP2_MOUSE Reviewed; 187 AA.
AC Q8VIN1; Q3KND5; Q8VIN0; Q9DA20;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Phosphatidylethanolamine-binding protein 2;
DE Short=PEBP-2;
GN Name=Pbp2; Synonyms=Pebp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=12193403; DOI=10.1095/biolreprod.101.001446;
RA Hickox D.M., Gibbs G., Morrison J.R., Sebire K., Edgar K., Keah H.-H.,
RA Alter K., Loveland K.L., Hearn M.T.W., de Kretser D.M., O'Bryan M.K.;
RT "Identification of a novel testis-specific member of the
RT phosphatidylethanolamine binding protein family, pebp-2.";
RL Biol. Reprod. 67:917-927(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-185.
RX PubMed=12037323; DOI=10.1107/s090744490200522x;
RA Simister P.C., Banfield M.J., Brady R.L.;
RT "The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family.";
RL Acta Crystallogr. D 58:1077-1080(2002).
CC -!- FUNCTION: May bind to phospholipids. May act as serine protease
CC inhibitor (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12193403}. Note=At
CC the cell periphery in pachytene spermatocytes and round spermatids, in
CC the distal dorsal region of the sperm head and in the sperm tail.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VIN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VIN1-2; Sequence=VSP_009738;
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12193403}.
CC -!- DEVELOPMENTAL STAGE: First detected 14 day old testes, with the first
CC appearance of stage IX pachytene spermatocytes. Highly expressed in
CC stage X and XI pachytene and diplotene spermatocytes from day 18 to 22.
CC -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC family. {ECO:0000305}.
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DR EMBL; AF307146; AAL32290.1; -; mRNA.
DR EMBL; AF307147; AAL32291.1; -; mRNA.
DR EMBL; BC107334; AAI07335.1; -; mRNA.
DR EMBL; BC107335; AAI07336.1; -; mRNA.
DR CCDS; CCDS20646.1; -. [Q8VIN1-1]
DR PDB; 1KN3; X-ray; 1.80 A; A=5-187.
DR PDBsum; 1KN3; -.
DR AlphaFoldDB; Q8VIN1; -.
DR SMR; Q8VIN1; -.
DR STRING; 10090.ENSMUSP00000098414; -.
DR MEROPS; I51.002; -.
DR MaxQB; Q8VIN1; -.
DR PaxDb; Q8VIN1; -.
DR PeptideAtlas; Q8VIN1; -.
DR PRIDE; Q8VIN1; -.
DR ProteomicsDB; 301787; -. [Q8VIN1-1]
DR ProteomicsDB; 301788; -. [Q8VIN1-2]
DR MGI; MGI:1923650; Pbp2.
DR eggNOG; KOG3346; Eukaryota.
DR InParanoid; Q8VIN1; -.
DR PhylomeDB; Q8VIN1; -.
DR ChiTaRS; Cbfb; mouse.
DR EvolutionaryTrace; Q8VIN1; -.
DR PRO; PR:Q8VIN1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VIN1; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd00866; PEBP_euk; 1.
DR Gene3D; 3.90.280.10; -; 1.
DR InterPro; IPR008914; PEBP.
DR InterPro; IPR036610; PEBP-like_sf.
DR InterPro; IPR035810; PEBP_euk.
DR InterPro; IPR001858; Phosphatidylethanolamine-bd_CS.
DR PANTHER; PTHR11362; PTHR11362; 1.
DR Pfam; PF01161; PBP; 1.
DR SUPFAM; SSF49777; SSF49777; 1.
DR PROSITE; PS01220; PBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Lipid-binding;
KW Nucleotide-binding; Phosphoprotein; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..187
FT /note="Phosphatidylethanolamine-binding protein 2"
FT /id="PRO_0000204747"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31044"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31044"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31044"
FT VAR_SEQ 99..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12193403"
FT /id="VSP_009738"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1KN3"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1KN3"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1KN3"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:1KN3"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:1KN3"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:1KN3"
SQ SEQUENCE 187 AA; 21191 MW; 9329E1490EC39B24 CRC64;
MPTDMSMWTG PLSLHEVDEQ PQHLLRVTYT EAEVEELGQV LTPTQVKHRP GSISWDGLDP
GKLYTLILTD PDAPSRKKPV YREWHHFLVV NMKGNDISSG NVLSDYVGSG PPKGTGLHRY
VWLVYQQDKP LRCDEPILTN RSGDHRGKFK TAAFRKKYHL GAPVAGTCYQ AEWDSYVPKL
YKQLSGK
