ID AKAP5_HUMAN Reviewed; 427 AA.
AC P24588; A2RRB8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 3.
DT 24-JAN-2024, entry version 199.
DE RecName: Full=A-kinase anchor protein 5;
DE Short=AKAP-5;
DE AltName: Full=A-kinase anchor protein 79 kDa;
DE Short=AKAP 79;
DE AltName: Full=H21;
DE AltName: Full=cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein;
GN Name=AKAP5; Synonyms=AKAP79;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS, AND VARIANT ILE-203.
RC TISSUE=Thyroid;
RX PubMed=1512224; DOI=10.1016/s0021-9258(18)41856-x;
RA Carr D.W., Stofko-Hahn R.E., Fraser I.D.C., Cone R.D., Scott J.D.;
RT "Localization of the cAMP-dependent protein kinase to the postsynaptic
RT densities by A-kinase anchoring proteins. Characterization of AKAP 79.";
RL J. Biol. Chem. 267:16816-16823(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-203.
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-203.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-203.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-427.
RC TISSUE=Kidney;
RX PubMed=1733921; DOI=10.1016/s0021-9258(18)45852-8;
RA Hirsch A.H., Glantz S.B., Li Y., You Y., Rubin C.S.;
RT "Cloning and expression of an intron-less gene for AKAP 75, an anchor
RT protein for the regulatory subunit of cAMP-dependent protein kinase II
RT beta.";
RL J. Biol. Chem. 267:2131-2134(1992).
RN [7]
RP PALMITOYLATION AT CYS-36 AND CYS-129, INTERACTION WITH ADCY8, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21771783; DOI=10.1074/jbc.m111.243899;
RA Delint-Ramirez I., Willoughby D., Hammond G.V., Ayling L.J., Cooper D.M.;
RT "Palmitoylation targets AKAP79 protein to lipid rafts and promotes its
RT regulation of calcium-sensitive adenylyl cyclase type 8.";
RL J. Biol. Chem. 286:32962-32975(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-36 AND CYS-129, AND
RP MUTAGENESIS OF CYS-36 AND CYS-129.
RX PubMed=25589740; DOI=10.1523/jneurosci.2243-14.2015;
RA Woolfrey K.M., Sanderson J.L., Dell'Acqua M.L.;
RT "The palmitoyl acyltransferase DHHC2 regulates recycling endosome
RT exocytosis and synaptic potentiation through palmitoylation of
RT AKAP79/150.";
RL J. Neurosci. 35:442-456(2015).
CC -!- FUNCTION: Multivalent scaffold protein that anchors the cAMP-dependent
CC protein kinase/PKA to cytoskeletal and/or organelle-associated
CC proteins, targeting the signal carried by cAMP to specific
CC intracellular effectors (PubMed:1512224). Association with the beta2-
CC adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling
CC pathway, but also the activation by PKA by switching off the beta2-AR
CC signaling cascade. Plays a role in long term synaptic potentiation by
CC regulating protein trafficking from the dendritic recycling endosomes
CC to the plasma membrane and controlling both structural and functional
CC plasticity at excitatory synapses (PubMed:25589740).
CC {ECO:0000269|PubMed:1512224, ECO:0000269|PubMed:25589740}.
CC -!- SUBUNIT: Binding protein for dimer of the RII-beta regulatory subunit
CC of cAMP-dependent protein kinase (PKA) and also for the protein kinase
CC C (PKC) and the phosphatase calcineurin (PP2B). Each enzyme is
CC inhibited when bound to the anchoring protein. Also binds the beta2-
CC adrenergic receptor. Part of a complex containing AKAP5, ADCY5, ADCY6
CC and PDE4C (By similarity). Interacts with ADCY8, and enhances its
CC phosphorylation at lipid rafts. {ECO:0000250,
CC ECO:0000269|PubMed:21771783}.
CC -!- INTERACTION:
CC P24588; Q08209-1: PPP3CA; NbExp=6; IntAct=EBI-703640, EBI-15637215;
CC P24588; Q08209-2: PPP3CA; NbExp=3; IntAct=EBI-703640, EBI-11959013;
CC P24588; P10644: PRKAR1A; NbExp=3; IntAct=EBI-703640, EBI-476431;
CC P24588; P13861: PRKAR2A; NbExp=5; IntAct=EBI-703640, EBI-2556122;
CC P24588; P31323: PRKAR2B; NbExp=4; IntAct=EBI-703640, EBI-2930670;
CC P24588; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-703640, EBI-1378139;
CC P24588; Q96C74: ROPN1L; NbExp=3; IntAct=EBI-703640, EBI-9033237;
CC P24588; Q9HBX9: RXFP1; NbExp=2; IntAct=EBI-703640, EBI-8088969;
CC P24588; P35561: Kcnj2; Xeno; NbExp=2; IntAct=EBI-703640, EBI-703793;
CC -!- SUBCELLULAR LOCATION: Postsynaptic recycling endosome membrane
CC {ECO:0000269|PubMed:21771783, ECO:0000269|PubMed:25589740}; Lipid-
CC anchor {ECO:0000269|PubMed:21771783}. Note=Associates with lipid rafts.
CC {ECO:0000269|PubMed:21771783}.
CC -!- TISSUE SPECIFICITY: Predominantly in the cerebral cortex and the
CC postsynaptic densities of the forebrain, and to a lesser extent in
CC adrenal medulla, lung and anterior pituitary.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
CC -!- DOMAIN: The N-terminal region, which is highly basic, is required for
CC interaction with calmodulin.
CC -!- PTM: Palmitoylated (PubMed:21771783, PubMed:25589740). Palmitoylation
CC at Cys-36 and Cys-129 play a key role in the targeting of AKAP5 to
CC lipid rafts (PubMed:21771783). Palmitoylation by ZDHHC2 is required for
CC AKAP5 function in LTP-stimulated recycling endosome exocytosis
CC (PubMed:25589740). {ECO:0000269|PubMed:21771783,
CC ECO:0000269|PubMed:25589740}.
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; M90359; AAA58363.1; -; mRNA.
DR EMBL; AK315336; BAG37736.1; -; mRNA.
DR EMBL; AL122035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80862.1; -; Genomic_DNA.
DR EMBL; BC131516; AAI31517.1; -; mRNA.
DR CCDS; CCDS9764.1; -.
DR PIR; A43453; A43453.
DR RefSeq; NP_004848.3; NM_004857.3.
DR PDB; 2H9R; NMR; -; C=391-412.
DR PDB; 3LL8; X-ray; 2.00 A; E=336-346.
DR PDB; 5NIN; X-ray; 1.70 A; C/D=77-92.
DR PDBsum; 2H9R; -.
DR PDBsum; 3LL8; -.
DR PDBsum; 5NIN; -.
DR AlphaFoldDB; P24588; -.
DR BMRB; P24588; -.
DR SMR; P24588; -.
DR BioGRID; 114874; 68.
DR ComplexPortal; CPX-1112; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant.
DR ComplexPortal; CPX-1114; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
DR ComplexPortal; CPX-1116; Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant.
DR ComplexPortal; CPX-1118; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant.
DR ComplexPortal; CPX-674; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
DR ComplexPortal; CPX-998; Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant.
DR CORUM; P24588; -.
DR DIP; DIP-186N; -.
DR IntAct; P24588; 37.
DR MINT; P24588; -.
DR STRING; 9606.ENSP00000378207; -.
DR TCDB; 8.A.28.1.6; the ankyrin (ankyrin) family.
DR iPTMnet; P24588; -.
DR PhosphoSitePlus; P24588; -.
DR SwissPalm; P24588; -.
DR BioMuta; AKAP5; -.
DR DMDM; 281185503; -.
DR jPOST; P24588; -.
DR MassIVE; P24588; -.
DR MaxQB; P24588; -.
DR PaxDb; 9606-ENSP00000378207; -.
DR PeptideAtlas; P24588; -.
DR ProteomicsDB; 54217; -.
DR Pumba; P24588; -.
DR Antibodypedia; 3806; 279 antibodies from 31 providers.
DR DNASU; 9495; -.
DR Ensembl; ENST00000320636.5; ENSP00000315615.5; ENSG00000179841.8.
DR Ensembl; ENST00000394718.4; ENSP00000378207.3; ENSG00000179841.8.
DR GeneID; 9495; -.
DR KEGG; hsa:9495; -.
DR MANE-Select; ENST00000394718.4; ENSP00000378207.3; NM_004857.3; NP_004848.3.
DR UCSC; uc001xhd.4; human.
DR AGR; HGNC:375; -.
DR CTD; 9495; -.
DR DisGeNET; 9495; -.
DR GeneCards; AKAP5; -.
DR HGNC; HGNC:375; AKAP5.
DR HPA; ENSG00000179841; Tissue enriched (brain).
DR MIM; 604688; gene.
DR neXtProt; NX_P24588; -.
DR OpenTargets; ENSG00000179841; -.
DR PharmGKB; PA24669; -.
DR VEuPathDB; HostDB:ENSG00000179841; -.
DR eggNOG; ENOG502S1NI; Eukaryota.
DR GeneTree; ENSGT00390000019941; -.
DR HOGENOM; CLU_052825_0_0_1; -.
DR InParanoid; P24588; -.
DR OMA; PCIKFSK; -.
DR OrthoDB; 5351313at2759; -.
DR PhylomeDB; P24588; -.
DR TreeFam; TF105404; -.
DR PathwayCommons; P24588; -.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-399719; Trafficking of AMPA receptors.
DR Reactome; R-HSA-9010642; ROBO receptors bind AKAP5.
DR SignaLink; P24588; -.
DR SIGNOR; P24588; -.
DR BioGRID-ORCS; 9495; 12 hits in 1150 CRISPR screens.
DR EvolutionaryTrace; P24588; -.
DR GeneWiki; AKAP5; -.
DR GenomeRNAi; 9495; -.
DR Pharos; P24588; Tbio.
DR PRO; PR:P24588; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P24588; Protein.
DR Bgee; ENSG00000179841; Expressed in middle temporal gyrus and 159 other cell types or tissues.
DR Genevisible; P24588; HS.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0060076; C:excitatory synapse; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IDA:UniProtKB.
DR GO; GO:0098944; C:postsynaptic recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; NAS:ComplexPortal.
DR GO; GO:0008179; F:adenylate cyclase binding; IPI:UniProtKB.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050811; F:GABA receptor binding; IBA:GO_Central.
DR GO; GO:0035254; F:glutamate receptor binding; IDA:SynGO-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0051018; F:protein kinase A binding; TAS:ProtInc.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:MGI.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IDA:SynGO-UCL.
DR GO; GO:0097110; F:scaffold protein binding; IPI:SynGO-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:SynGO-UCL.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IMP:UniProtKB.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; NAS:ComplexPortal.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; NAS:ComplexPortal.
DR GO; GO:1905751; P:positive regulation of endosome to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR IDEAL; IID00233; -.
DR InterPro; IPR042375; AKAP5.
DR InterPro; IPR001573; AKAP_WSK.
DR PANTHER; PTHR15182:SF0; A-KINASE ANCHOR PROTEIN 5; 1.
DR PANTHER; PTHR15182; A-KINASE ANCHOR PROTEIN 5-RELATED; 1.
DR Pfam; PF03832; WSK; 1.
DR PROSITE; PS51893; AKAP_CAM_BD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Endosome; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..427
FT /note="A-kinase anchor protein 5"
FT /id="PRO_0000064529"
FT REGION 1..170
FT /note="Essential to the intracellular anchoring function"
FT /evidence="ECO:0000250"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..405
FT /note="PKA-RII subunit binding domain"
FT MOTIF 76..96
FT /note="AKAP CaM-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3YVF0"
FT LIPID 36
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21771783"
FT LIPID 129
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21771783"
FT VARIANT 100
FT /note="P -> L (in dbSNP:rs2230491)"
FT /id="VAR_056732"
FT VARIANT 203
FT /note="T -> I (in dbSNP:rs1256149)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:1512224, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_060735"
FT VARIANT 314
FT /note="E -> K (in dbSNP:rs34433837)"
FT /id="VAR_056733"
FT MUTAGEN 36
FT /note="C->S: Loss of palmitoylation by ZDHHC2; when
FT associated with S-129."
FT /evidence="ECO:0000269|PubMed:25589740"
FT MUTAGEN 129
FT /note="C->S: Loss of palmitoylation by ZDHHC2; when
FT associated with S-36."
FT /evidence="ECO:0000269|PubMed:25589740"
FT MUTAGEN 392
FT /note="L->P: Prevents or diminishes RII binding."
FT /evidence="ECO:0000269|PubMed:1512224"
FT MUTAGEN 396
FT /note="A->P: Prevents or diminishes RII binding."
FT /evidence="ECO:0000269|PubMed:1512224"
FT MUTAGEN 400
FT /note="V->P: Prevents or diminishes RII binding."
FT /evidence="ECO:0000269|PubMed:1512224"
FT MUTAGEN 405
FT /note="Q->P: Prevents or diminishes RII binding."
FT /evidence="ECO:0000269|PubMed:1512224"
FT MUTAGEN 408
FT /note="I->P: Prevents or diminishes RII binding."
FT /evidence="ECO:0000269|PubMed:1512224"
FT CONFLICT 188
FT /note="R -> Q (in Ref. 1; AAA58363)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="S -> Y (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:5NIN"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:3LL8"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:2H9R"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:2H9R"
SQ SEQUENCE 427 AA; 47088 MW; D2A86298EAF1BE32 CRC64;
METTISEIHV ENKDEKRSAE GSPGAERQKE KASMLCFKRR KKAAKALKPK AGSEAADVAR
KCPQEAGASD QPEPTRGAWA SLKRLVTRRK RSESSKQQKP LEGEMQPAIN AEDADLSKKK
AKSRLKIPCI KFPRGPKRSN HSKIIEDSDC SIKVQEEAEI LDIQTQTPLN DQATKAKSTQ
DLSEGISRKD GDEVCESNVS NSTTSGEKVI SVELGLDNGH SAIQTGTLIL EEIETIKEKQ
DVQPQQASPL ETSETDHQQP VLSDVPPLPA IPDQQIVEEA SNSTLESAPN GKDYESTEIV
AEETKPKDTE LSQESDFKEN GITEEKSKSE ESKRMEPIAI IITDTEISEF DVTKSKNVPK
QFLISAENEQ VGVFANDNGF EDRTSEQYET LLIETASSLV KNAIQLSIEQ LVNEMASDDN
KINNLLQ
//
