Full text data of GDA
GDA
(KIAA1258)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Guanine deaminase; Guanase; Guanine aminase; 3.5.4.3 (Guanine aminohydrolase; GAH; p51-nedasin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Guanine deaminase; Guanase; Guanine aminase; 3.5.4.3 (Guanine aminohydrolase; GAH; p51-nedasin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00465184
IPI00465184 KIAA1258 protein zinc binding, Guanine deaminase activity, nucleotide and nucleic acid metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a intracellular n/a found at its expected molecular weight found at molecular weight
IPI00465184 KIAA1258 protein zinc binding, Guanine deaminase activity, nucleotide and nucleic acid metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a intracellular n/a found at its expected molecular weight found at molecular weight
UniProt
Q9Y2T3
ID GUAD_HUMAN Reviewed; 454 AA.
AC Q9Y2T3; B4DTY5; Q5SZC7; Q9H335; Q9ULG2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Guanine deaminase;
DE Short=Guanase;
DE Short=Guanine aminase;
DE EC=3.5.4.3;
DE AltName: Full=Guanine aminohydrolase;
DE Short=GAH;
DE AltName: Full=p51-nedasin;
GN Name=GDA; Synonyms=KIAA1258;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10075721; DOI=10.1074/jbc.274.12.8175;
RA Yuan G., Bin J.C., McKay D.J., Snyder F.F.;
RT "Cloning and characterization of human guanine deaminase. Purification
RT and partial amino acid sequence of the mouse protein.";
RL J. Biol. Chem. 274:8175-8180(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10542258; DOI=10.1074/jbc.274.45.32204;
RA Kuwahara H., Araki N., Makino K., Masuko N., Honda S., Kaibuchi K.,
RA Fukunaga K., Miyamoto E., Ogawa M., Saya H.;
RT "A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the
RT amidohydrolase superfamily, interferes with the association between
RT NE-dlg/SAP102 and N-methyl-D-aspartate receptor.";
RL J. Biol. Chem. 274:32204-32214(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Park K.H., Seong Y.S., Park J.B.;
RT "Molecular cloning of human guanine aminohydrolase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP XANTHINE.
RG Structural genomics consortium (SGC);
RT "Human guanine deaminase (GUAD) in complex with zinc and its product
RT xanthine.";
RL Submitted (JAN-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine,
CC producing xanthine and ammonia (By similarity).
CC -!- CATALYTIC ACTIVITY: Guanine + H(2)O = xanthine + NH(3).
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from
CC guanine: step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2T3-1; Sequence=Displayed;
CC Name=2; Synonyms=c;
CC IsoId=Q9Y2T3-2; Sequence=VSP_042075;
CC Name=3; Synonyms=a;
CC IsoId=Q9Y2T3-3; Sequence=VSP_042076;
CC -!- SIMILARITY: Belongs to the ATZ/TRZ family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86572.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AF095286; AAD25978.1; -; mRNA.
DR EMBL; AF019638; AAF13301.1; -; mRNA.
DR EMBL; AF144745; AAG40469.1; -; mRNA.
DR EMBL; AB033084; BAA86572.1; ALT_INIT; mRNA.
DR EMBL; AK300418; BAG62147.1; -; mRNA.
DR EMBL; AK315988; BAH14359.1; -; mRNA.
DR EMBL; AL583829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590311; CAI12631.1; -; Genomic_DNA.
DR EMBL; AL135924; CAI12631.1; JOINED; Genomic_DNA.
DR EMBL; AL135924; CAI16261.1; -; Genomic_DNA.
DR EMBL; AL590311; CAI16261.1; JOINED; Genomic_DNA.
DR EMBL; CH471089; EAW62529.1; -; Genomic_DNA.
DR EMBL; BC053584; AAH53584.1; -; mRNA.
DR RefSeq; NP_001229434.1; NM_001242505.2.
DR RefSeq; NP_001229435.1; NM_001242506.2.
DR RefSeq; NP_001229436.1; NM_001242507.2.
DR RefSeq; NP_004284.1; NM_004293.4.
DR RefSeq; XP_005252374.1; XM_005252317.1.
DR UniGene; Hs.494163; -.
DR PDB; 2UZ9; X-ray; 2.30 A; A=1-454.
DR PDB; 3E0L; X-ray; 2.37 A; A/B=1-454.
DR PDB; 4AQL; X-ray; 1.99 A; A=1-454.
DR PDBsum; 2UZ9; -.
DR PDBsum; 3E0L; -.
DR PDBsum; 4AQL; -.
DR ProteinModelPortal; Q9Y2T3; -.
DR SMR; Q9Y2T3; 8-451.
DR MINT; MINT-109340; -.
DR STRING; 9606.ENSP00000351170; -.
DR BindingDB; Q9Y2T3; -.
DR ChEMBL; CHEMBL3129; -.
DR MEROPS; M38.981; -.
DR PhosphoSite; Q9Y2T3; -.
DR DMDM; 9910736; -.
DR PaxDb; Q9Y2T3; -.
DR PRIDE; Q9Y2T3; -.
DR DNASU; 9615; -.
DR Ensembl; ENST00000238018; ENSP00000238018; ENSG00000119125.
DR Ensembl; ENST00000358399; ENSP00000351170; ENSG00000119125.
DR Ensembl; ENST00000475764; ENSP00000436619; ENSG00000119125.
DR Ensembl; ENST00000545168; ENSP00000437972; ENSG00000119125.
DR GeneID; 9615; -.
DR KEGG; hsa:9615; -.
DR UCSC; uc004aiq.3; human.
DR CTD; 9615; -.
DR GeneCards; GC09P074729; -.
DR HGNC; HGNC:4212; GDA.
DR HPA; HPA019352; -.
DR HPA; HPA024099; -.
DR HPA; HPA030387; -.
DR MIM; 139260; gene.
DR neXtProt; NX_Q9Y2T3; -.
DR PharmGKB; PA28625; -.
DR eggNOG; COG0402; -.
DR HOGENOM; HOG000257692; -.
DR HOVERGEN; HBG005930; -.
DR InParanoid; Q9Y2T3; -.
DR KO; K01487; -.
DR OMA; CEAFYHA; -.
DR PhylomeDB; Q9Y2T3; -.
DR BioCyc; MetaCyc:HS04276-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00603; UER00660.
DR EvolutionaryTrace; Q9Y2T3; -.
DR GenomeRNAi; 9615; -.
DR NextBio; 36069; -.
DR PRO; PR:Q9Y2T3; -.
DR ArrayExpress; Q9Y2T3; -.
DR Bgee; Q9Y2T3; -.
DR CleanEx; HS_GDA; -.
DR Genevestigator; Q9Y2T3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008892; F:guanine deaminase activity; EXP:Reactome.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
DR InterPro; IPR006680; Amidohydro_1.
DR InterPro; IPR014311; Guanine_deaminase.
DR PANTHER; PTHR11271:SF6; PTHR11271:SF6; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1 454 Guanine deaminase.
FT /FTId=PRO_0000122298.
FT METAL 82 82 Zinc; via tele nitrogen.
FT METAL 84 84 Zinc; via tele nitrogen.
FT METAL 240 240 Zinc; via tele nitrogen.
FT METAL 330 330 Zinc (By similarity).
FT BINDING 87 87 Substrate.
FT BINDING 213 213 Substrate.
FT BINDING 243 243 Substrate.
FT BINDING 279 279 Substrate.
FT VAR_SEQ 1 74 Missing (in isoform 2).
FT /FTId=VSP_042075.
FT VAR_SEQ 454 454 V -> VKETIHLPASSPHPPPFP (in isoform 3).
FT /FTId=VSP_042076.
FT CONFLICT 316 318 LEV -> ARI (in Ref. 3; AAG40469).
FT STRAND 11 19
FT STRAND 27 36
FT STRAND 40 47
FT HELIX 48 50
FT HELIX 51 57
FT HELIX 62 64
FT STRAND 65 67
FT STRAND 73 76
FT STRAND 78 84
FT HELIX 85 90
FT HELIX 99 105
FT HELIX 107 112
FT HELIX 113 115
FT HELIX 117 133
FT STRAND 136 142
FT HELIX 147 160
FT STRAND 163 167
FT STRAND 175 177
FT HELIX 184 201
FT STRAND 204 208
FT STRAND 210 212
FT TURN 215 217
FT HELIX 220 232
FT STRAND 237 242
FT HELIX 245 254
FT STRAND 258 260
FT HELIX 261 266
FT TURN 267 269
FT STRAND 275 279
FT HELIX 285 294
FT STRAND 297 300
FT HELIX 302 307
FT HELIX 315 320
FT STRAND 324 327
FT TURN 331 333
FT HELIX 339 355
FT STRAND 358 361
FT HELIX 365 372
FT HELIX 374 379
FT TURN 383 385
FT STRAND 386 388
FT STRAND 397 400
FT HELIX 414 417
FT STRAND 418 420
FT HELIX 423 431
FT HELIX 434 436
FT STRAND 437 442
FT STRAND 445 448
SQ SEQUENCE 454 AA; 51003 MW; A45C868E6EEA7380 CRC64;
MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF
KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL EWLTKYTFPA EHRFQNIDFA
EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MDLNDTFPEY
KETTEESIKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH
ISENRDEVEA VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH
CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE
KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI
SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV
//
ID GUAD_HUMAN Reviewed; 454 AA.
AC Q9Y2T3; B4DTY5; Q5SZC7; Q9H335; Q9ULG2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Guanine deaminase;
DE Short=Guanase;
DE Short=Guanine aminase;
DE EC=3.5.4.3;
DE AltName: Full=Guanine aminohydrolase;
DE Short=GAH;
DE AltName: Full=p51-nedasin;
GN Name=GDA; Synonyms=KIAA1258;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10075721; DOI=10.1074/jbc.274.12.8175;
RA Yuan G., Bin J.C., McKay D.J., Snyder F.F.;
RT "Cloning and characterization of human guanine deaminase. Purification
RT and partial amino acid sequence of the mouse protein.";
RL J. Biol. Chem. 274:8175-8180(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10542258; DOI=10.1074/jbc.274.45.32204;
RA Kuwahara H., Araki N., Makino K., Masuko N., Honda S., Kaibuchi K.,
RA Fukunaga K., Miyamoto E., Ogawa M., Saya H.;
RT "A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the
RT amidohydrolase superfamily, interferes with the association between
RT NE-dlg/SAP102 and N-methyl-D-aspartate receptor.";
RL J. Biol. Chem. 274:32204-32214(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Park K.H., Seong Y.S., Park J.B.;
RT "Molecular cloning of human guanine aminohydrolase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP XANTHINE.
RG Structural genomics consortium (SGC);
RT "Human guanine deaminase (GUAD) in complex with zinc and its product
RT xanthine.";
RL Submitted (JAN-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine,
CC producing xanthine and ammonia (By similarity).
CC -!- CATALYTIC ACTIVITY: Guanine + H(2)O = xanthine + NH(3).
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from
CC guanine: step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2T3-1; Sequence=Displayed;
CC Name=2; Synonyms=c;
CC IsoId=Q9Y2T3-2; Sequence=VSP_042075;
CC Name=3; Synonyms=a;
CC IsoId=Q9Y2T3-3; Sequence=VSP_042076;
CC -!- SIMILARITY: Belongs to the ATZ/TRZ family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86572.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF095286; AAD25978.1; -; mRNA.
DR EMBL; AF019638; AAF13301.1; -; mRNA.
DR EMBL; AF144745; AAG40469.1; -; mRNA.
DR EMBL; AB033084; BAA86572.1; ALT_INIT; mRNA.
DR EMBL; AK300418; BAG62147.1; -; mRNA.
DR EMBL; AK315988; BAH14359.1; -; mRNA.
DR EMBL; AL583829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590311; CAI12631.1; -; Genomic_DNA.
DR EMBL; AL135924; CAI12631.1; JOINED; Genomic_DNA.
DR EMBL; AL135924; CAI16261.1; -; Genomic_DNA.
DR EMBL; AL590311; CAI16261.1; JOINED; Genomic_DNA.
DR EMBL; CH471089; EAW62529.1; -; Genomic_DNA.
DR EMBL; BC053584; AAH53584.1; -; mRNA.
DR RefSeq; NP_001229434.1; NM_001242505.2.
DR RefSeq; NP_001229435.1; NM_001242506.2.
DR RefSeq; NP_001229436.1; NM_001242507.2.
DR RefSeq; NP_004284.1; NM_004293.4.
DR RefSeq; XP_005252374.1; XM_005252317.1.
DR UniGene; Hs.494163; -.
DR PDB; 2UZ9; X-ray; 2.30 A; A=1-454.
DR PDB; 3E0L; X-ray; 2.37 A; A/B=1-454.
DR PDB; 4AQL; X-ray; 1.99 A; A=1-454.
DR PDBsum; 2UZ9; -.
DR PDBsum; 3E0L; -.
DR PDBsum; 4AQL; -.
DR ProteinModelPortal; Q9Y2T3; -.
DR SMR; Q9Y2T3; 8-451.
DR MINT; MINT-109340; -.
DR STRING; 9606.ENSP00000351170; -.
DR BindingDB; Q9Y2T3; -.
DR ChEMBL; CHEMBL3129; -.
DR MEROPS; M38.981; -.
DR PhosphoSite; Q9Y2T3; -.
DR DMDM; 9910736; -.
DR PaxDb; Q9Y2T3; -.
DR PRIDE; Q9Y2T3; -.
DR DNASU; 9615; -.
DR Ensembl; ENST00000238018; ENSP00000238018; ENSG00000119125.
DR Ensembl; ENST00000358399; ENSP00000351170; ENSG00000119125.
DR Ensembl; ENST00000475764; ENSP00000436619; ENSG00000119125.
DR Ensembl; ENST00000545168; ENSP00000437972; ENSG00000119125.
DR GeneID; 9615; -.
DR KEGG; hsa:9615; -.
DR UCSC; uc004aiq.3; human.
DR CTD; 9615; -.
DR GeneCards; GC09P074729; -.
DR HGNC; HGNC:4212; GDA.
DR HPA; HPA019352; -.
DR HPA; HPA024099; -.
DR HPA; HPA030387; -.
DR MIM; 139260; gene.
DR neXtProt; NX_Q9Y2T3; -.
DR PharmGKB; PA28625; -.
DR eggNOG; COG0402; -.
DR HOGENOM; HOG000257692; -.
DR HOVERGEN; HBG005930; -.
DR InParanoid; Q9Y2T3; -.
DR KO; K01487; -.
DR OMA; CEAFYHA; -.
DR PhylomeDB; Q9Y2T3; -.
DR BioCyc; MetaCyc:HS04276-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00603; UER00660.
DR EvolutionaryTrace; Q9Y2T3; -.
DR GenomeRNAi; 9615; -.
DR NextBio; 36069; -.
DR PRO; PR:Q9Y2T3; -.
DR ArrayExpress; Q9Y2T3; -.
DR Bgee; Q9Y2T3; -.
DR CleanEx; HS_GDA; -.
DR Genevestigator; Q9Y2T3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008892; F:guanine deaminase activity; EXP:Reactome.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
DR InterPro; IPR006680; Amidohydro_1.
DR InterPro; IPR014311; Guanine_deaminase.
DR PANTHER; PTHR11271:SF6; PTHR11271:SF6; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1 454 Guanine deaminase.
FT /FTId=PRO_0000122298.
FT METAL 82 82 Zinc; via tele nitrogen.
FT METAL 84 84 Zinc; via tele nitrogen.
FT METAL 240 240 Zinc; via tele nitrogen.
FT METAL 330 330 Zinc (By similarity).
FT BINDING 87 87 Substrate.
FT BINDING 213 213 Substrate.
FT BINDING 243 243 Substrate.
FT BINDING 279 279 Substrate.
FT VAR_SEQ 1 74 Missing (in isoform 2).
FT /FTId=VSP_042075.
FT VAR_SEQ 454 454 V -> VKETIHLPASSPHPPPFP (in isoform 3).
FT /FTId=VSP_042076.
FT CONFLICT 316 318 LEV -> ARI (in Ref. 3; AAG40469).
FT STRAND 11 19
FT STRAND 27 36
FT STRAND 40 47
FT HELIX 48 50
FT HELIX 51 57
FT HELIX 62 64
FT STRAND 65 67
FT STRAND 73 76
FT STRAND 78 84
FT HELIX 85 90
FT HELIX 99 105
FT HELIX 107 112
FT HELIX 113 115
FT HELIX 117 133
FT STRAND 136 142
FT HELIX 147 160
FT STRAND 163 167
FT STRAND 175 177
FT HELIX 184 201
FT STRAND 204 208
FT STRAND 210 212
FT TURN 215 217
FT HELIX 220 232
FT STRAND 237 242
FT HELIX 245 254
FT STRAND 258 260
FT HELIX 261 266
FT TURN 267 269
FT STRAND 275 279
FT HELIX 285 294
FT STRAND 297 300
FT HELIX 302 307
FT HELIX 315 320
FT STRAND 324 327
FT TURN 331 333
FT HELIX 339 355
FT STRAND 358 361
FT HELIX 365 372
FT HELIX 374 379
FT TURN 383 385
FT STRAND 386 388
FT STRAND 397 400
FT HELIX 414 417
FT STRAND 418 420
FT HELIX 423 431
FT HELIX 434 436
FT STRAND 437 442
FT STRAND 445 448
SQ SEQUENCE 454 AA; 51003 MW; A45C868E6EEA7380 CRC64;
MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF
KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL EWLTKYTFPA EHRFQNIDFA
EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MDLNDTFPEY
KETTEESIKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH
ISENRDEVEA VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH
CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE
KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI
SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV
//
MIM
139260
*RECORD*
*FIELD* NO
139260
*FIELD* TI
*139260 GUANINE DEAMINASE; GDA
;;GUANASE;;
CYTOPLASMIC PSD95 INTERACTOR; CYPIN
*FIELD* TX
read more
DESCRIPTION
Guanine deaminase (GDA; EC 3.5.4.3) catalyzes the hydrolytic deamination
of guanine, producing xanthine and ammonia.
CLONING
Yuan et al. (1999) searched an EST database with peptide sequences of
purified mouse GDA and identified a human EST encoding a homolog. Using
this EST, they isolated a full-length human brain GDA cDNA. The open
reading frame of the cDNA predicts a 51-kD, 454-amino acid protein
containing a 9-residue N-terminal motif that is present in other
aminohydrolases and amidohydrolases.
Using a PSD95 (602887) protein column for affinity chromatography,
Firestein et al. (1999) isolated a PSD95-binding protein, which they
named cypin, in rat brain extracts. They cloned a cypin cDNA from a rat
brain cDNA library. Northern blot analysis identified expression of
cypin in rat brain, liver, and spleen as well as in human brain, liver,
and kidney. No expression was detected in human heart, lung, skeletal
muscle, or pancreas.
Harris et al. (1974) found no genetic variants by electrophoretic means.
GENE FUNCTION
Firestein et al. (1999) found that in rat brain, cypin occurs discretely
in several neuronal populations in forebrain, but is completely absent
from hindbrain and spinal cord. Cypin localizes to both pre- and
postsynaptic sites, is enriched in dendritic shafts, cofractionates, and
associates with membrane-associated guanylate kinase proteins (PSD95/93
and SAP97/102) in the synaptic plasma membranes and vesicles. Cypin also
occurs in the epithelial cells of the small intestine, highest at the
tips of the intestinal villi, and exclusively at the basal membrane. GST
fusion experiments showed that cypin binding to PSD95 occurs through a
C-terminal consensus sequence and requires PDZ domains 1 and 2.
Overexpression of cypin in rat hippocampal neurons specifically perturbs
postsynaptic trafficking of PSD95 and SAP102 (300189), an effect not
produced by overexpression of other PDZ ligands. Firestein et al. (1999)
suggested that cypin may influence synaptic development and plasticity
by regulating postsynaptic protein sorting.
In cultured rat hippocampal neurons, Akum et al. (2004) found that cypin
is expressed in developing dendrites and increases its expression in
axons as the neurons mature. Overexpression of cypin resulted in a
significant increase in both primary and secondary dendrites, whereas
mutant cypin without guanine deaminase activity acted as a dominant
negative and resulted in decreased dendrite number. Akum et al. (2004)
used 5-prime end-mutated U1 mammalian small nuclear RNA (U1 snRNA;
180680) to inhibit cypin mRNA maturation and protein expression, which
also resulted in fewer dendrites. Cypin was found to bind to tubulin
heterodimers and promote microtubule assembly.
*FIELD* RF
1. Akum, B. F.; Chen, M.; Gunderson, S. I.; Riefler, G. M.; Scerri-Hansen,
M. M.; Firestein, B. L.: Cypin regulates dendrite patterning in hippocampal
neurons by promoting microtubule assembly. Nature Neurosci. 7: 145-152,
2004.
2. Firestein, B. L.; Brenman, J. E.; Aoki, C.; Sanchez-Perez, A. M.;
El-Husseini, A. E.-D.; Bredt, D. S.: Cypin: a cytosolic regulator
of PSD-95 postsynaptic targeting. Neuron 24: 659-672, 1999.
3. Harris, H.; Hopkinson, D. A.; Robson, E. B.: The incidence of
rare alleles determining electrophoretic variants: data on 43 enzyme
loci in man. Ann. Hum. Genet. 37: 237-253, 1974.
4. Yuan, G.; Bin, J. C.; McKay, D. J.; Snyder, F. F.: Cloning and
characterization of human guanine deaminase: purification and partial
amino acid sequence of the mouse protein. J. Biol. Chem. 274: 8175-8180,
1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 2/24/2004
Wilson H. Y. Lo - updated: 4/7/2000
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 07/13/2004
tkritzer: 3/4/2004
ckniffin: 2/24/2004
carol: 1/21/2004
terry: 4/7/2000
carol: 10/1/1999
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/4/1986
*RECORD*
*FIELD* NO
139260
*FIELD* TI
*139260 GUANINE DEAMINASE; GDA
;;GUANASE;;
CYTOPLASMIC PSD95 INTERACTOR; CYPIN
*FIELD* TX
read more
DESCRIPTION
Guanine deaminase (GDA; EC 3.5.4.3) catalyzes the hydrolytic deamination
of guanine, producing xanthine and ammonia.
CLONING
Yuan et al. (1999) searched an EST database with peptide sequences of
purified mouse GDA and identified a human EST encoding a homolog. Using
this EST, they isolated a full-length human brain GDA cDNA. The open
reading frame of the cDNA predicts a 51-kD, 454-amino acid protein
containing a 9-residue N-terminal motif that is present in other
aminohydrolases and amidohydrolases.
Using a PSD95 (602887) protein column for affinity chromatography,
Firestein et al. (1999) isolated a PSD95-binding protein, which they
named cypin, in rat brain extracts. They cloned a cypin cDNA from a rat
brain cDNA library. Northern blot analysis identified expression of
cypin in rat brain, liver, and spleen as well as in human brain, liver,
and kidney. No expression was detected in human heart, lung, skeletal
muscle, or pancreas.
Harris et al. (1974) found no genetic variants by electrophoretic means.
GENE FUNCTION
Firestein et al. (1999) found that in rat brain, cypin occurs discretely
in several neuronal populations in forebrain, but is completely absent
from hindbrain and spinal cord. Cypin localizes to both pre- and
postsynaptic sites, is enriched in dendritic shafts, cofractionates, and
associates with membrane-associated guanylate kinase proteins (PSD95/93
and SAP97/102) in the synaptic plasma membranes and vesicles. Cypin also
occurs in the epithelial cells of the small intestine, highest at the
tips of the intestinal villi, and exclusively at the basal membrane. GST
fusion experiments showed that cypin binding to PSD95 occurs through a
C-terminal consensus sequence and requires PDZ domains 1 and 2.
Overexpression of cypin in rat hippocampal neurons specifically perturbs
postsynaptic trafficking of PSD95 and SAP102 (300189), an effect not
produced by overexpression of other PDZ ligands. Firestein et al. (1999)
suggested that cypin may influence synaptic development and plasticity
by regulating postsynaptic protein sorting.
In cultured rat hippocampal neurons, Akum et al. (2004) found that cypin
is expressed in developing dendrites and increases its expression in
axons as the neurons mature. Overexpression of cypin resulted in a
significant increase in both primary and secondary dendrites, whereas
mutant cypin without guanine deaminase activity acted as a dominant
negative and resulted in decreased dendrite number. Akum et al. (2004)
used 5-prime end-mutated U1 mammalian small nuclear RNA (U1 snRNA;
180680) to inhibit cypin mRNA maturation and protein expression, which
also resulted in fewer dendrites. Cypin was found to bind to tubulin
heterodimers and promote microtubule assembly.
*FIELD* RF
1. Akum, B. F.; Chen, M.; Gunderson, S. I.; Riefler, G. M.; Scerri-Hansen,
M. M.; Firestein, B. L.: Cypin regulates dendrite patterning in hippocampal
neurons by promoting microtubule assembly. Nature Neurosci. 7: 145-152,
2004.
2. Firestein, B. L.; Brenman, J. E.; Aoki, C.; Sanchez-Perez, A. M.;
El-Husseini, A. E.-D.; Bredt, D. S.: Cypin: a cytosolic regulator
of PSD-95 postsynaptic targeting. Neuron 24: 659-672, 1999.
3. Harris, H.; Hopkinson, D. A.; Robson, E. B.: The incidence of
rare alleles determining electrophoretic variants: data on 43 enzyme
loci in man. Ann. Hum. Genet. 37: 237-253, 1974.
4. Yuan, G.; Bin, J. C.; McKay, D. J.; Snyder, F. F.: Cloning and
characterization of human guanine deaminase: purification and partial
amino acid sequence of the mouse protein. J. Biol. Chem. 274: 8175-8180,
1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 2/24/2004
Wilson H. Y. Lo - updated: 4/7/2000
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 07/13/2004
tkritzer: 3/4/2004
ckniffin: 2/24/2004
carol: 1/21/2004
terry: 4/7/2000
carol: 10/1/1999
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/4/1986