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Database: UniProt
Entry: M3X9U5_FELCA
LinkDB: M3X9U5_FELCA
Original site: M3X9U5_FELCA 
ID   M3X9U5_FELCA            Unreviewed;       568 AA.
AC   M3X9U5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 3.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Protein phosphatase 1 regulatory subunit 16B {ECO:0000313|Ensembl:ENSFCAP00000023398.3};
GN   Name=PPP1R16B {ECO:0000313|Ensembl:ENSFCAP00000023398.3,
GN   ECO:0000313|VGNC:VGNC:64321};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000023398.3, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000023398.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000023398.3,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000023398.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000023398.3,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000023398.3}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000023398.3};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
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DR   EMBL; AANG04003379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3X9U5; -.
DR   STRING; 9685.ENSFCAP00000023398; -.
DR   PaxDb; 9685-ENSFCAP00000023398; -.
DR   Ensembl; ENSFCAT00000030622.4; ENSFCAP00000023398.3; ENSFCAG00000022215.4.
DR   VGNC; VGNC:64321; PPP1R16B.
DR   eggNOG; KOG0505; Eukaryota.
DR   GeneTree; ENSGT00940000154090; -.
DR   HOGENOM; CLU_000134_54_2_1; -.
DR   InParanoid; M3X9U5; -.
DR   OMA; QQLKVWR; -.
DR   Proteomes; UP000011712; Chromosome A3.
DR   Bgee; ENSFCAG00000022215; Expressed in prefrontal cortex and 9 other cell types or tissues.
DR   GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR   GO; GO:0017020; F:myosin phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IBA:GO_Central.
DR   GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IEA:Ensembl.
DR   GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
DR   GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:1903670; P:regulation of sprouting angiogenesis; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR017417; Pase-1_reg_su_16AB.
DR   PANTHER; PTHR24179:SF31; PROTEIN PHOSPHATASE 1 REGULATORY INHIBITOR SUBUNIT 16B; 1.
DR   PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   PIRSF; PIRSF038159; PP1_16AB_vert; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023289};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT   PROPEP          566..568
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
FT                   /id="PRO_5036528124"
FT   REPEAT          100..132
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          133..165
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          228..260
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          261..293
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          373..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         565
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
FT   LIPID           564
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
FT   LIPID           565
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
SQ   SEQUENCE   568 AA;  63595 MW;  878D25F0EC801919 CRC64;
     MASHVDLLTE LQLLEKVPTL ERLRAAQKRR AQQLKKWAQY EQDLQHRKRK HERKRSTGGR
     RKKVSFEASV ALLEASLRND AEEVRYFLKN KVSPDLCNED GLTALHQCCI DNFEEIVKLL
     LSHGANVNAK DNELWTPLHA AATCGHINLV KILVQYGADL LAVNSDGNMP YDLCEDEPTL
     DVIETCMAYQ GITQEKINEM RAAPEQQMIA DIHCMIAAGQ DLDWIDAQGA TLLHIAGANG
     YLRAAELLLD HGVRVDVKDW DGWEPLHAAA FWGQMQMAEL LVSHGASLSA RTSMDEMPID
     LCEEEEFKVL LLELKHKHDV IMKSQLRHKS SLSRRTSSAG SRGKVVRRAS LSDRTNLYRK
     EYEGEAILWQ QRSAAEDQRT SAYNGDIRET RTDQENKDPN PRLEKPVLLS EFSTKIPRSE
     MDGPVENGLR APVSTYQYAL SNGDVWKVHE VPDYNMAYGS PGVADATSPW SGYKEQSPQT
     LLELKRQRAA AKLLSHPFLS THLGSSMGRT GESSSEGKAP LIGGRTSPYS SNGTSVYYTV
     TSGDPPLLKF KAPMEEMEEK VHGCCRIS
//
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