RHBG_HUMAN
ID RHBG_HUMAN Reviewed; 458 AA.
AC Q9H310; A8K475; Q5SZW4; Q5SZW6; Q5SZW7; Q6P193; Q6YJI2; Q6YJI3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ammonium transporter Rh type B {ECO:0000305};
DE AltName: Full=Rhesus blood group family type B glycoprotein;
DE Short=Rh family type B glycoprotein;
DE Short=Rh type B glycoprotein;
GN Name=RHBG {ECO:0000312|HGNC:HGNC:14572};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=11024028; DOI=10.1074/jbc.m007528200;
RA Liu Z., Peng J., Mo R., Hui C.-C., Huang C.-H.;
RT "Rh type B glycoprotein is a new member of the Rh superfamily and a
RT putative ammonia transporter in mammals.";
RL J. Biol. Chem. 276:1424-1433(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Liver;
RA Liu Z., Chen Y., Huang C.-H.;
RT "Characterization of alternatively spliced Rh type B glycoprotein (RhBG)
RT isoforms in human tissues resulting from exonic inclusion of Alu repeat
RT like sequences.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT ASP-76.
RC TISSUE=Cerebellum, and Liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-76.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ASP-143
RP AND ARG-315.
RC TISSUE=Ovary;
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 [7]
RP FUNCTION.
RX PubMed=15284342; DOI=10.1113/jphysiol.2004.067728;
RA Ludewig U.;
RT "Electroneutral ammonium transport by basolateral rhesus B glycoprotein.";
RL J. Physiol. (Lond.) 559:751-759(2004).
RN [8]
RP FUNCTION.
RX PubMed=15929723; DOI=10.1042/bj20050657;
RA Zidi-Yahiaoui N., Mouro-Chanteloup I., D'Ambrosio A.-M., Lopez C., Gane P.,
RA Le van Kim C., Cartron J.-P., Colin Y., Ripoche P.;
RT "Human Rhesus B and Rhesus C glycoproteins: properties of facilitated
RT ammonium transport in recombinant kidney cells.";
RL Biochem. J. 391:33-40(2005).
RN [9]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-419; LEU-420 AND ASP-421, AND
RP INTERACTION WITH ANK2 AND ANK3.
RX PubMed=15611082; DOI=10.1074/jbc.m413351200;
RA Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R.,
RA Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.;
RT "The ammonium transporter RhBG: requirement of a tyrosine-based signal and
RT ankyrin-G for basolateral targeting and membrane anchorage in polarized
RT kidney epithelial cells.";
RL J. Biol. Chem. 280:8221-8228(2005).
CC -!- FUNCTION: Functions as a specific ammonium transporter.
CC {ECO:0000269|PubMed:15284342, ECO:0000269|PubMed:15929723}.
CC -!- SUBUNIT: Interacts (via C-terminus) with ANK2 and ANK3; required for
CC targeting to the basolateral membrane. {ECO:0000269|PubMed:15611082}.
CC -!- INTERACTION:
CC Q9H310-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12006870, EBI-3867333;
CC Q9H310-3; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-12006870, EBI-12811111;
CC Q9H310-3; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-12006870, EBI-12196745;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H310-1; Sequence=Displayed;
CC Name=2; Synonyms=RhBG-2A;
CC IsoId=Q9H310-2; Sequence=VSP_024341, VSP_024342;
CC Name=3;
CC IsoId=Q9H310-3; Sequence=VSP_024340, VSP_024343;
CC Name=4; Synonyms=RhBG-1A;
CC IsoId=Q9H310-4; Sequence=VSP_024340;
CC Name=5;
CC IsoId=Q9H310-5; Sequence=VSP_024340, VSP_037136;
CC -!- TISSUE SPECIFICITY: Specifically expressed in kidney. Also detected in
CC liver and ovary. {ECO:0000269|PubMed:11024028}.
CC -!- DEVELOPMENTAL STAGE: Fetally expressed by kidney and to a lower extent
CC in liver. {ECO:0000269|PubMed:11024028}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65218.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF193807; AAG01086.1; -; mRNA.
DR EMBL; AF219980; AAL05978.1; -; Genomic_DNA.
DR EMBL; AF219977; AAL05978.1; JOINED; Genomic_DNA.
DR EMBL; AF219978; AAL05978.1; JOINED; Genomic_DNA.
DR EMBL; AF219979; AAL05978.1; JOINED; Genomic_DNA.
DR EMBL; AY139092; AAN34363.1; -; mRNA.
DR EMBL; AY139093; AAN34364.1; -; mRNA.
DR EMBL; AK054780; BAG51423.1; -; mRNA.
DR EMBL; AK290840; BAF83529.1; -; mRNA.
DR EMBL; AL139130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52961.1; -; Genomic_DNA.
DR EMBL; BC065218; AAH65218.1; ALT_FRAME; mRNA.
DR CCDS; CCDS41414.2; -. [Q9H310-1]
DR RefSeq; NP_001243324.1; NM_001256395.1.
DR RefSeq; NP_001243325.1; NM_001256396.1.
DR RefSeq; NP_065140.3; NM_020407.4.
DR AlphaFoldDB; Q9H310; -.
DR BioGRID; 121390; 4.
DR CORUM; Q9H310; -.
DR IntAct; Q9H310; 4.
DR STRING; 9606.ENSP00000441197; -.
DR TCDB; 1.A.11.4.2; the ammonium transporter channel (amt) family.
DR GlyGen; Q9H310; 1 site.
DR PhosphoSitePlus; Q9H310; -.
DR BioMuta; RHBG; -.
DR DMDM; 209572666; -.
DR MassIVE; Q9H310; -.
DR PaxDb; Q9H310; -.
DR PeptideAtlas; Q9H310; -.
DR PRIDE; Q9H310; -.
DR Antibodypedia; 34214; 129 antibodies from 26 providers.
DR DNASU; 57127; -.
DR Ensembl; ENST00000537040.6; ENSP00000441197.2; ENSG00000132677.13. [Q9H310-1]
DR GeneID; 57127; -.
DR KEGG; hsa:57127; -.
DR MANE-Select; ENST00000537040.6; ENSP00000441197.2; NM_020407.5; NP_065140.3.
DR UCSC; uc031vbi.2; human. [Q9H310-1]
DR CTD; 57127; -.
DR DisGeNET; 57127; -.
DR GeneCards; RHBG; -.
DR HGNC; HGNC:14572; RHBG.
DR HPA; ENSG00000132677; Tissue enriched (kidney).
DR MIM; 607079; gene.
DR neXtProt; NX_Q9H310; -.
DR OpenTargets; ENSG00000132677; -.
DR PharmGKB; PA34385; -.
DR VEuPathDB; HostDB:ENSG00000132677; -.
DR eggNOG; KOG3796; Eukaryota.
DR GeneTree; ENSGT00950000182844; -.
DR HOGENOM; CLU_021386_0_0_1; -.
DR InParanoid; Q9H310; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q9H310; -.
DR TreeFam; TF314450; -.
DR PathwayCommons; Q9H310; -.
DR Reactome; R-HSA-444411; Rhesus glycoproteins mediate ammonium transport.
DR SignaLink; Q9H310; -.
DR BioGRID-ORCS; 57127; 13 hits in 222 CRISPR screens.
DR ChiTaRS; RHBG; human.
DR GeneWiki; RHBG; -.
DR GenomeRNAi; 57127; -.
DR Pharos; Q9H310; Tbio.
DR PRO; PR:Q9H310; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H310; protein.
DR Bgee; ENSG00000132677; Expressed in cerebellar cortex and 110 other tissues.
DR ExpressionAtlas; Q9H310; baseline and differential.
DR Genevisible; Q9H310; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IMP:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0030506; F:ankyrin binding; IPI:UniProtKB.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IDA:UniProtKB.
DR GO; GO:0070634; P:transepithelial ammonium transport; IDA:UniProtKB.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR InterPro; IPR002229; RhesusRHD.
DR Pfam; PF00909; Ammonium_transp; 1.
DR PRINTS; PR00342; RHESUSRHD.
PE 1: Evidence at protein level;
KW Alternative splicing; Ammonia transport; Cell membrane;
KW Cytoplasmic vesicle; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..458
FT /note="Ammonium transporter Rh type B"
FT /id="PRO_0000283597"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 416..424
FT /note="Interaction with ANK3"
FT /evidence="ECO:0000269|PubMed:15611082"
FT REGION 436..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_024340"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024341"
FT VAR_SEQ 31..63
FT /note="AVFVRYNHKTDAALWHRSNHSNADNEFYFRYPS -> MNFTFATQKSLTLLP
FT RLECNGAISAHCNLHLPG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024342"
FT VAR_SEQ 175
FT /note="G -> GVRVWGGMESGVGGGQGQPLSQERGGGGGVLPLTPPPQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024343"
FT VAR_SEQ 372..458
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037136"
FT VARIANT 76
FT /note="G -> D (in dbSNP:rs2245623)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_031497"
FT VARIANT 143
FT /note="V -> D (in dbSNP:rs11586833)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031498"
FT VARIANT 315
FT /note="G -> R (in dbSNP:rs3748569)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031499"
FT VARIANT 339
FT /note="C -> R (in dbSNP:rs3748567)"
FT /id="VAR_053637"
FT MUTAGEN 419
FT /note="F->A: Loss of interaction with ANK3. Intracellular
FT retention; when associated with A-420 and A-421."
FT /evidence="ECO:0000269|PubMed:15611082"
FT MUTAGEN 420
FT /note="L->A: Partial loss of interaction with ANK3.
FT Intracellular retention; when associated with A-419 and A-
FT 421."
FT /evidence="ECO:0000269|PubMed:15611082"
FT MUTAGEN 421
FT /note="D->A: Partial loss of interaction with ANK3.
FT Intracellular retention; when associated with A-419 and A-
FT 420."
FT /evidence="ECO:0000269|PubMed:15611082"
FT CONFLICT 428
FT /note="H -> R (in Ref. 6; AAH65218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 49481 MW; 8266F94B637DEF93 CRC64;
MAGSPSRAAG RRLQLPLLCL FLQGATAVLF AVFVRYNHKT DAALWHRSNH SNADNEFYFR
YPSFQDVHAM VFVGFGFLMV FLQRYGFSSV GFTFLLAAFA LQWSTLVQGF LHSFHGGHIH
VGVESMINAD FCAGAVLISF GAVLGKTGPT QLLLMALLEV VLFGINEFVL LHLLGVRDAG
GSMTIHTFGA YFGLVLSRVL YRPQLEKSKH RQGSVYHSDL FAMIGTIFLW IFWPSFNAAL
TALGAGQHRT ALNTYYSLAA STLGTFALSA LVGEDGRLDM VHIQNAALAG GVVVGTSSEM
MLTPFGALAA GFLAGTVSTL GYKFFTPILE SKFKVQDTCG VHNLHGMPGV LGALLGVLVA
GLATHEAYGD GLESVFPLIA EGQRSATSQA MHQLFGLFVT LMFASVGGGL GGLLLKLPFL
DSPPDSQHYE DQVHWQVPGE HEDKAQRPLR VEEADTQA
