PHLB1_RAT
ID PHLB1_RAT Reviewed; 831 AA.
AC Q63312;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Pleckstrin homology-like domain family B member 1;
DE AltName: Full=Protein LL5-alpha;
DE Flags: Fragment;
GN Name=Phldb1; Synonyms=Ll5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pituitary;
RX PubMed=8241284; DOI=10.1016/0167-4781(93)90171-9;
RA Levi L., Hanukoglu I., Raikhinstein M., Kohen F., Koch Y.;
RT "Cloning of LL5, a novel protein-encoding cDNA from a rat pituitary
RT library.";
RL Biochim. Biophys. Acta 1216:342-344(1993).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-27; SER-33;
RP SER-45; SER-72 AND SER-77, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- DOMAIN: The PH domain mediates the binding to phosphoinositides.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52297.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X74226; CAA52297.1; ALT_SEQ; mRNA.
DR PIR; S37032; S37032.
DR AlphaFoldDB; Q63312; -.
DR SMR; Q63312; -.
DR IntAct; Q63312; 1.
DR STRING; 10116.ENSRNOP00000046235; -.
DR CarbonylDB; Q63312; -.
DR iPTMnet; Q63312; -.
DR jPOST; Q63312; -.
DR PRIDE; Q63312; -.
DR UCSC; RGD:620878; rat.
DR RGD; 620878; Phldb1.
DR eggNOG; ENOG502QPZY; Eukaryota.
DR InParanoid; Q63312; -.
DR PhylomeDB; Q63312; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045180; C:basal cortex; ISO:RGD.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:RGD.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0010470; P:regulation of gastrulation; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:RGD.
DR CDD; cd14673; PH_PHLDB1_2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037810; PHLDB1/2/3_PH.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN <1..831
FT /note="Pleckstrin homology-like domain family B member 1"
FT /id="PRO_0000053893"
FT DOMAIN 721..824
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..306
FT /evidence="ECO:0000255"
FT COILED 610..676
FT /evidence="ECO:0000255"
FT COMPBIAS 33..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDH0"
FT NON_TER 1
SQ SEQUENCE 831 AA; 93541 MW; 16AFCA423765E596 CRC64;
LTLGARGRRT RSPSPTLGES LAPRKGSFSG RLSPAYSLGS LTGASPRQSP HAQRKLSSGD
LRVPIPRERK NSITEISDNE DDLLEYHRRQ RQERLREQEM ERLERQRLET ILNLCAEYSR
ADGGPETGEL PSIGEATAAL ALAGRRPSRG LAGAIVVSGR SGEESGGASQ RLWESMERSD
EENLKEECSS TESTQQEHED APSTKLQGEV LAVEEERAQV LGRVEQLKVR VKELEQQLQE
AAREAEMERA LLQGEREAER ALLQKEQRAM DQLQEKLVAL ETGIQKERDK EADALETETK
LFEDLEFQQL ERESRVEEER ELAGQGLLRS KAELLRSVSK RKERLAVLDS QAGQIRAQAV
QESERLAREK NAVLQLLQKE KEKLTVLERR YHSLTGGRPF PKTTSTLKEV YRSKMNGDMA
SPLPRTRSGP LPSSSGSSSS SSQLSVATLG RSPSPKSALL AQNGTSSLPR NLAATLQDIE
TKRQLALQQK VELPPAEPLS PEDPAGHQVI EEQRRRLAEL KQKAAAEAQC QWDALHGAAA
FPAGPSGFPT LMHHSILHHL PAGRERGEEG EHAYDTLSLE SSDSMETSIS TGGNSACSPD
NMSSASGLDM GKIEEMEKML KEAHAEKSRL MESREREMEL RRQALEEERR RREQVERRLQ
SESARRQQLV EKEVKLREKQ FSQARPLTRY LPNRKEDFDL KTHIESSGHG VDTCLHVVLS
SKVCRGYLIK MGGKIKSWKK RWFVFDRLKR TLSYYVDKHE TKLKGVIYFQ AIEEVYYDHL
RSAAKSPNPA LTFCVKTHDR LYYMVAPSAE AMRIWMDVIV TGAEGYTQFM N
