ID H3CNL9_TETNG Unreviewed; 553 AA.
AC H3CNL9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Protein phosphatase 1, regulatory subunit 16B {ECO:0000313|Ensembl:ENSTNIP00000009851.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000009851.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000009851.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; H3CNL9; -.
DR STRING; 99883.ENSTNIP00000009851; -.
DR Ensembl; ENSTNIT00000010029.1; ENSTNIP00000009851.1; ENSTNIG00000007051.1.
DR GeneTree; ENSGT00940000154090; -.
DR HOGENOM; CLU_000134_54_2_1; -.
DR InParanoid; H3CNL9; -.
DR OMA; QQLKVWR; -.
DR TreeFam; TF316803; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
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 PRINTS; PR01415; ANKYRIN.
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:UP000007303}.
FT PROPEP 551..553
FT /note="Removed in mature form"
FT /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
FT /id="PRO_5036529094"
FT REPEAT 105..137
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 138..170
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 233..265
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 266..298
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 550
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
FT LIPID 549
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
FT LIPID 550
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038159-50"
SQ SEQUENCE 553 AA; 61432 MW; 5820A8CD465C3630 CRC64;
MANHLELIQE LQQLDKAPSL ERLRAAQKRR TQQLKRWAVY EKEMQSKKRK ADKKARSANS
LQQDHKKHVS FAASVALLEA SARNDPDEVR YLLTNNVSAD LCNEDGLTAL HQCCIDNYEE
MVKILLDRGA NVNAQDNELW TPLHAAATCG HAGLVIILIA YGADLLAVNS DGNMPYDLCE
DDPTLDIIET AMANRGITQE MINETRASTE RRMLRDIQEL LKQGEEVNQQ DSQGATLLHV
AAANGYVQAT ELLLEGGARM DLRDSDGWQA LHAAACWGQM HVAELLVSHG ASLNAKTFLE
ETPIDLCEDE EFRAILLDLK HKHDTIMKSQ LKHKTSLCRR TSSAGSRGKV VRRASLSDRH
NLCRKEYETE AIVWRGGREE EPEKERESDQ ENNQTVQDSK FCNPKSFFVP QVKALTSVEQ
PDQPRLQTIL KDSAGTQNGL ISTATSTPAP LPSNGSVPTP EMGSQPPQEE AWPKERAQTL
SELKKQRAAA KLLNHPYTPS LMPNPPRRTP ACPLVSSNGS AVYYTPASGD PPLLKLKQPE
EEQPKAQTCC CVS
//
