PP1R7_BOVIN
ID PP1R7_BOVIN Reviewed; 360 AA.
AC Q3T0W4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 7;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 22;
GN Name=PPP1R7; Synonyms=SDS22;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 6-20; 223-241; 322-330 AND 352-359, FUNCTION,
RP INTERACTION WITH PPP1CC ISOFORM 2, AND TISSUE SPECIFICITY.
RX PubMed=12444072; DOI=10.1095/biolreprod.102.004093;
RA Huang Z., Khatra B., Bollen M., Carr D.W., Vijayaraghavan S.;
RT "Sperm PP1gamma2 is regulated by a homologue of the yeast protein
RT phosphatase binding protein sds22.";
RL Biol. Reprod. 67:1936-1942(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH PPP1CC ISOFORM 2.
RX PubMed=12826576; DOI=10.1095/biolreprod.103.018739;
RA Mishra S., Somanath P.R., Huang Z., Vijayaraghavan S.;
RT "Binding and inactivation of the germ cell-specific protein phosphatase
RT PP1gamma2 by sds22 during epididymal sperm maturation.";
RL Biol. Reprod. 69:1572-1579(2003).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 1. Inactivates the
CC PPP1CC isoform 2 during epididymal sperm maturation.
CC {ECO:0000269|PubMed:12444072, ECO:0000269|PubMed:12826576}.
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G (By
CC similarity). Interacts with PPP1CC isoform 2 in motile caudal
CC epididymal spermatozoa. {ECO:0000250, ECO:0000269|PubMed:12444072,
CC ECO:0000269|PubMed:12826576}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in epididymal spermatozoa including the
CC principal piece of the flagellum and the head-neck junction.
CC {ECO:0000269|PubMed:12444072}.
CC -!- SIMILARITY: Belongs to the SDS22 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102228; AAI02229.1; -; mRNA.
DR RefSeq; NP_001029410.1; NM_001034238.2.
DR AlphaFoldDB; Q3T0W4; -.
DR SMR; Q3T0W4; -.
DR STRING; 9913.ENSBTAP00000001045; -.
DR PaxDb; Q3T0W4; -.
DR PeptideAtlas; Q3T0W4; -.
DR PRIDE; Q3T0W4; -.
DR Ensembl; ENSBTAT00000001045; ENSBTAP00000001045; ENSBTAG00000000789.
DR GeneID; 505297; -.
DR KEGG; bta:505297; -.
DR CTD; 5510; -.
DR VEuPathDB; HostDB:ENSBTAG00000000789; -.
DR VGNC; VGNC:52808; PPP1R7.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000162473; -.
DR HOGENOM; CLU_044236_1_1_1; -.
DR InParanoid; Q3T0W4; -.
DR OMA; YDNLIAH; -.
DR OrthoDB; 968788at2759; -.
DR TreeFam; TF105538; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000000789; Expressed in pons and 103 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR Pfam; PF12799; LRR_4; 2.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 11.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Leucine-rich repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT CHAIN 2..360
FT /note="Protein phosphatase 1 regulatory subunit 7"
FT /id="PRO_0000239612"
FT REPEAT 77..98
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 121..142
FT /note="LRR 3"
FT REPEAT 143..164
FT /note="LRR 4"
FT REPEAT 165..186
FT /note="LRR 5"
FT REPEAT 187..208
FT /note="LRR 6"
FT REPEAT 209..230
FT /note="LRR 7"
FT REPEAT 231..252
FT /note="LRR 8"
FT REPEAT 253..274
FT /note="LRR 9"
FT REPEAT 275..296
FT /note="LRR 10"
FT REPEAT 297..318
FT /note="LRR 11"
FT DOMAIN 331..360
FT /note="LRRCT"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
SQ SEQUENCE 360 AA; 41388 MW; 021091E11AE4C7A9 CRC64;
MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKQNSGMV ADLSAHSLKD GEERGDEDPE
EGQELPVDME TISLDRDAED VDLNHYRIGK IEGFEVLKKV KTLCLRQNLI KCIENLEGLQ
SLRELDLYDN QIRRIENLDA LTELEVLDIS FNLLRNIEGI DKLTRLKKLF LVNNKINKIE
NISSLHQLQM LELGSNRIRA IENIDTLTNL ESLFLGKNKI TKLQNLDALT NLTVLSMQSN
RLTKIEGLQS LVNLRELYLS HNGIEVIEGL DNNNKLTMLD IASNRIKKIE NVSHLTELQE
FWMNDNLLDC WSDLDELKGA RSLETVYLER NPLQRDPQYR RKIMLALPSV RQIDATFVRF
