PRAM_MOUSE
ID PRAM_MOUSE Reviewed; 675 AA.
AC Q6BCL1; E9QL42;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=PML-RARA-regulated adapter molecule 1;
DE Short=PRAM-1;
GN Name=Pram1;
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], TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=15572693; DOI=10.1128/mcb.24.24.10923-10932.2004;
RA Clemens R.A., Newbrough S.A., Chung E.Y., Gheith S., Singer A.L.,
RA Koretzky G.A., Peterson E.J.;
RT "PRAM-1 is required for optimal integrin-dependent neutrophil function.";
RL Mol. Cell. Biol. 24:10923-10932(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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).
CC -!- FUNCTION: May be involved in integrin signaling in neutrophils. Binds
CC to PtdIns(4)P. {ECO:0000269|PubMed:15572693}.
CC -!- SUBUNIT: Interacts with SKAP2, LCP2 and DBNL. May interact with LYN (By
CC similarity). Interacts with NEK6 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow and mature neutrophils.
CC Weakly expressed in macrophages and mast cells.
CC {ECO:0000269|PubMed:15572693}.
CC -!- DOMAIN: The SH3 domain binds to PtdIns(4)P. {ECO:0000250}.
CC -!- PTM: May be phosphorylated on tyrosines. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are healthy and do not display any obvious
CC abnormality. They have normal hematopoietic differentiation.
CC {ECO:0000269|PubMed:15572693}.
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DR EMBL; AY665714; AAT76049.1; -; mRNA.
DR EMBL; CT033847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37569.1; -.
DR RefSeq; NP_001002842.2; NM_001002842.2.
DR AlphaFoldDB; Q6BCL1; -.
DR SMR; Q6BCL1; -.
DR STRING; 10090.ENSMUSP00000057065; -.
DR iPTMnet; Q6BCL1; -.
DR PhosphoSitePlus; Q6BCL1; -.
DR MaxQB; Q6BCL1; -.
DR PaxDb; Q6BCL1; -.
DR PRIDE; Q6BCL1; -.
DR ProteomicsDB; 289883; -.
DR Antibodypedia; 24911; 124 antibodies from 25 providers.
DR DNASU; 378460; -.
DR Ensembl; ENSMUST00000052079; ENSMUSP00000057065; ENSMUSG00000032739.
DR GeneID; 378460; -.
DR KEGG; mmu:378460; -.
DR UCSC; uc008byz.1; mouse.
DR CTD; 84106; -.
DR MGI; MGI:3576625; Pram1.
DR VEuPathDB; HostDB:ENSMUSG00000032739; -.
DR eggNOG; ENOG502SS22; Eukaryota.
DR GeneTree; ENSGT00530000063460; -.
DR HOGENOM; CLU_460488_0_0_1; -.
DR InParanoid; Q6BCL1; -.
DR OMA; IVIQTRM; -.
DR OrthoDB; 203958at2759; -.
DR PhylomeDB; Q6BCL1; -.
DR TreeFam; TF337003; -.
DR BioGRID-ORCS; 378460; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pram1; mouse.
DR PRO; PR:Q6BCL1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6BCL1; protein.
DR Bgee; ENSMUSG00000032739; Expressed in granulocyte and 58 other tissues.
DR ExpressionAtlas; Q6BCL1; baseline and differential.
DR Genevisible; Q6BCL1; MM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; 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:0007229; P:integrin-mediated signaling pathway; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0043313; P:regulation of neutrophil degranulation; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR043443; FYB1/2-like.
DR InterPro; IPR029294; hSH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR16830; PTHR16830; 1.
DR Pfam; PF14603; hSH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Lipid-binding; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..675
FT /note="PML-RARA-regulated adapter molecule 1"
FT /id="PRO_0000270172"
FT DOMAIN 578..656
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 537
FT /note="L -> P (in Ref. 1; AAT76049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 75508 MW; CD5A2A14949B1732 CRC64;
MGSNQDFRNL QAKFQTSQPE LGELFRKTPK PELNKVLKKF PQTELSEQPK KSSQSELSAV
SLKPLQLQFA DLPRKPPQPG VLKKSPQPEF PHLANKPVQA EFPRKPLHPE FTGLKKPSQA
EFTDLKKPPQ PQFASLPKKP PKPEFGELSK RPPQLETPQE PSAPPAQKLL KPEPNNPARP
LGELKPKMFW HLEANEAPKR PLPSESSTFP KKPLQPEAVV GFSRKSQPQS ESIEVSQTSP
SKCGSRELDS HSPQPDISTF PKNNENFRKP SYPQATGCPK SPKQPMFYEF PQTPPRKPES
CNPQSHSPLP DFNAFPKKHP QLQPSDLTRA SSEPEVCKVP KKTQKPDPNV LSQKPSQPEL
GHLPRTSSDP EFNSLPRKFL QPQHGKFFQP EFPKGLPRKP KLPGSVSECS LPSASAGSSP
QCPLSPGLIV PGIPRWRSED FQVQRPPRRR PLPSASSLGH PPAKPALPPG PINIQSFRRA
AATAAAVLKT GSSTGTHFQA QQPQHIAQNP DEIYELYDAV EATDDSSISP RGRDEMLSTQ
QATRWPQQEP ELRKKATQPQ QLPATDPKLL KQIRKAEKAE REFRKKFKFE GEIVIHTKMM
IDPNAKTRRG GGKHLGIRRG EILEVIEFTS KDEMLCRDPK GKYGYVPRTA LLPLETEVYD
DVSFGDPLDM QPFPR
