PK1IP_BOVIN
ID PK1IP_BOVIN Reviewed; 392 AA.
AC Q5EA99;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=p21-activated protein kinase-interacting protein 1;
DE AltName: Full=PAK1-interacting protein 1;
GN Name=PAK1IP1;
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).
CC -!- FUNCTION: Negatively regulates the PAK1 kinase. PAK1 is a member of the
CC PAK kinase family, which has been shown to play a positive role in the
CC regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists
CC as an inactive homodimer, which is activated by binding of small
CC GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also
CC binds to the N-terminus of PAK1, and inhibits the specific activation
CC of PAK1 by CDC42. May be involved in ribosomal large subunit assembly.
CC {ECO:0000250|UniProtKB:Q9NWT1}.
CC -!- SUBUNIT: Interacts with PAK1. {ECO:0000250|UniProtKB:Q9NWT1}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9NWT1}.
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DR EMBL; BT020668; AAX08685.1; -; mRNA.
DR EMBL; BT020670; AAX08687.1; -; mRNA.
DR RefSeq; NP_001014852.1; NM_001014852.1.
DR AlphaFoldDB; Q5EA99; -.
DR SMR; Q5EA99; -.
DR STRING; 9913.ENSBTAP00000024854; -.
DR PaxDb; Q5EA99; -.
DR PeptideAtlas; Q5EA99; -.
DR GeneID; 505125; -.
DR KEGG; bta:505125; -.
DR CTD; 55003; -.
DR eggNOG; KOG0294; Eukaryota.
DR InParanoid; Q5EA99; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repeat; Ribosome biogenesis;
KW Signal transduction inhibitor; WD repeat.
FT CHAIN 1..392
FT /note="p21-activated protein kinase-interacting protein 1"
FT /id="PRO_0000051124"
FT REPEAT 40..77
FT /note="WD 1"
FT REPEAT 80..118
FT /note="WD 2"
FT REPEAT 121..160
FT /note="WD 3"
FT REPEAT 202..240
FT /note="WD 4"
FT REPEAT 243..284
FT /note="WD 5"
FT REGION 309..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..392
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 44049 MW; CC2B64D833D3E3F6 CRC64;
MEVVAGCYEQ VLFGFAVHPE PVGDGHRERW APVADFTHHA HTASLSAVAV NSRFVVTGSK
DETIHIYDMK KKVDHGALMH HNGTITCLKF HGNRHLISGA EDGLICVWDA RRWECLKSIR
AHKGHVTFLS IHPSGRLALS VGTDKTLRTW NLVEGRSAFI KNIKQSAHIV EWSPKGEKYV
VVILNRIDVY QLDTASVSGT ITNERRVSSV TFLSESVLTV AGDEEVVRFF DCDSLTCLSE
FKAHENRVKD MFSFETPEHH VLVTASSDGF IKMWKLKQDK KVSPSLLCEI NTNARLTCLG
VWLDRRTDTK ESPPAAAEPA PVSKEQSRRN KEESGHAVQE EEKQPKPDTE KCSLTGDSNK
PTRGNSLVSA KKRKTVEMLE KKRKKKKIRM MQ