PRR14_BOVIN
ID PRR14_BOVIN Reviewed; 587 AA.
AC Q0VBZ8; Q58D02;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Proline-rich protein 14;
GN Name=PRR14;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in tethering peripheral heterochromatin to the
CC nuclear lamina during interphase, possibly through the interaction with
CC heterochromatin protein CBX5/HP1 alpha. Might play a role in
CC reattaching heterochromatin to the nuclear lamina at mitotic exit.
CC Promotes myoblast differentiation during skeletal myogenesis, possibly
CC by stimulating transcription factor MyoD activity via binding to
CC CBX5/HP1 alpha. Involved in the positive regulation of the PI3K-Akt-
CC mTOR signaling pathway and in promoting cell proliferation, possibly
CC via binding to GRB2 (By similarity). {ECO:0000250|UniProtKB:Q9BWN1}.
CC -!- SUBUNIT: Interacts (via proline-rich region) with GRB2 (via SH3 domain
CC 2). Interacts (via N-terminus) with CBX5.
CC {ECO:0000250|UniProtKB:Q9BWN1}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9BWN1}.
CC Nucleus {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus lamina
CC {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9BWN1}. Note=During interphase, associated with
CC peripheral heterochromatin at the nuclear lamina. Released from the
CC nuclear lamina in mitotic prophase and remains highly dispersed in
CC metaphase. Associates with chromatin at the onset of anaphase and
CC relocalizes to the nuclear lamina in telophase.
CC {ECO:0000250|UniProtKB:Q9BWN1}.
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DR EMBL; BT021795; AAX46642.1; -; mRNA.
DR EMBL; BC120423; AAI20424.1; -; mRNA.
DR RefSeq; NP_001030473.1; NM_001035396.1.
DR AlphaFoldDB; Q0VBZ8; -.
DR STRING; 9913.ENSBTAP00000011995; -.
DR PaxDb; Q0VBZ8; -.
DR PRIDE; Q0VBZ8; -.
DR Ensembl; ENSBTAT00000074947; ENSBTAP00000069502; ENSBTAG00000009099.
DR GeneID; 533235; -.
DR KEGG; bta:533235; -.
DR CTD; 78994; -.
DR VEuPathDB; HostDB:ENSBTAG00000009099; -.
DR VGNC; VGNC:33391; PRR14.
DR eggNOG; ENOG502RJ6E; Eukaryota.
DR GeneTree; ENSGT00520000055626; -.
DR HOGENOM; CLU_489653_0_0_1; -.
DR InParanoid; Q0VBZ8; -.
DR OrthoDB; 484832at2759; -.
DR TreeFam; TF328446; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000009099; Expressed in oocyte and 104 other tissues.
DR ExpressionAtlas; Q0VBZ8; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR InterPro; IPR026320; PRR14.
DR InterPro; IPR028149; Tantalus-like.
DR PANTHER; PTHR14522; PTHR14522; 1.
DR Pfam; PF15386; Tantalus; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; Myogenesis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..587
FT /note="Proline-rich protein 14"
FT /id="PRO_0000307268"
FT REGION 1..135
FT /note="Sufficient for heterochromatin association in
FT interphase and chromatin association in anaphase"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..378
FT /note="Required for the interaction with GRB2 and
FT sufficient to promote the phosphorylation of AKT and cell
FT proliferation"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 136..365
FT /note="Required for nuclear lamina association"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 178..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..536
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 524..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT CONFLICT 392
FT /note="A -> G (in Ref. 1; AAX46642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 64437 MW; 633499B63260202A CRC64;
MDLPGDSSTP GRQRLCRQPH AGALWGAKSP KRPKLQPLGA PSPLEKASRR VLAVVLEDVM
AARMVPLEPQ EESSTPRHHS NHRDSVRSQP PASPPRQAMW SPQARPPDPL HLCREPLSRI
RRPPSTPRRQ SRTTPGPDEG PSQKVDQVHQ PTLVVMLQDI ASSRPRAEGF ADEAPNFIIP
ARRAEPKVMV HQPKPPSRDL PAPSRPSALS ANPLASPPPA PDPVLEPPST PPPSSLLRPR
LSPWGLAPLF HSVRSKLESF ADIFLTPNKA PRPPPPSPPM KLELKIAISE AGQPGASEGT
VTVSPRPPIR QWRAQDQNPS ATLTKPSLGR SHSCPDLGPP GPDPCSWPPV PAPSSRPRPR
RHTVGGGEMA KAPPPPRPCL RKEVFPLGGV GASPPLVTSC SSTASTSSFS EPAEPRLSST
KRKEPRAPED QVLPDSETKT IGKVSRFRIR RTPARSQINL TPMGLPRPVR LNKKEFSLEE
IYTNKNYQSP TTRRTFETIF EEPRERNGTL IFTSSRKLRR TVEFRDSSLP RSRRPSRGAR
ATAGRTLPPS LAPSPDVEPL LQQRLQELDA SLLEEEEEGD QDQPHRT
