Full text data of PRPS1L1
PRPS1L1
(PRPS3, PRPSL)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ribose-phosphate pyrophosphokinase 3; 2.7.6.1 (Phosphoribosyl pyrophosphate synthase 1-like 1; PRPS1-like 1; Phosphoribosyl pyrophosphate synthase III; PRS-III)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribose-phosphate pyrophosphokinase 3; 2.7.6.1 (Phosphoribosyl pyrophosphate synthase 1-like 1; PRPS1-like 1; Phosphoribosyl pyrophosphate synthase III; PRS-III)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00218371
IPI00218371 phosphoribosyl pyrophosphate synthetase 1-like 1 phosphoribosyl pyrophosphate synthetase 1-like 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00218371 phosphoribosyl pyrophosphate synthetase 1-like 1 phosphoribosyl pyrophosphate synthetase 1-like 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
P21108
ID PRPS3_HUMAN Reviewed; 318 AA.
AC P21108; Q6P5P6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 3;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 1-like 1;
DE Short=PRPS1-like 1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase III;
DE Short=PRS-III;
GN Name=PRPS1L1; Synonyms=PRPS3, PRPSL;
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], AND PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Testis;
RX PubMed=2168892;
RA Taira M., Iizasa T., Shimada H., Kudoh J., Shimizu N., Tatibana M.;
RT "A human testis-specific mRNA for phosphoribosylpyrophosphate
RT synthetase that initiates from a non-AUG codon.";
RL J. Biol. Chem. 265:16491-16497(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-279.
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate
CC (PRPP) that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Activated by magnesium and inorganic phosphate.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed
CC of 3 homodimers (By similarity).
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
CC -!- CAUTION: According to PubMed:2168892, this sequence initiates from
CC a non-AUG codon; N-terminal ACG codon did serve as a start codon.
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DR EMBL; M57423; AAB59463.1; -; mRNA.
DR EMBL; BC062797; AAH62797.2; -; mRNA.
DR PIR; A37893; KIHUR3.
DR RefSeq; NP_787082.1; NM_175886.2.
DR UniGene; Hs.169284; -.
DR ProteinModelPortal; P21108; -.
DR SMR; P21108; 3-313.
DR STRING; 9606.ENSP00000390134; -.
DR PhosphoSite; P21108; -.
DR DMDM; 125585; -.
DR SWISS-2DPAGE; P21108; -.
DR PRIDE; P21108; -.
DR GeneID; 221823; -.
DR KEGG; hsa:221823; -.
DR UCSC; uc003stz.3; human.
DR CTD; 221823; -.
DR GeneCards; GC07M018066; -.
DR H-InvDB; HIX0033604; -.
DR HGNC; HGNC:9463; PRPS1L1.
DR MIM; 611566; gene.
DR neXtProt; NX_P21108; -.
DR PharmGKB; PA33818; -.
DR HOGENOM; HOG000210451; -.
DR HOVERGEN; HBG001520; -.
DR InParanoid; P21108; -.
DR KO; K00948; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00087; UER00172.
DR GenomeRNAi; 221823; -.
DR NextBio; 91465; -.
DR PRO; PR:P21108; -.
DR CleanEx; HS_PRPS1L1; -.
DR Genevestigator; P21108; -.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; ISS:UniProtKB.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; NAS:UniProtKB.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Direct protein sequencing; Kinase;
KW Magnesium; Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW Polymorphism; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 318 Ribose-phosphate pyrophosphokinase 3.
FT /FTId=PRO_0000141078.
FT NP_BIND 96 101 ATP (By similarity).
FT REGION 212 227 Binding of phosphoribosylpyrophosphate
FT (Potential).
FT METAL 128 128 Magnesium (Potential).
FT METAL 130 130 Magnesium (Potential).
FT METAL 139 139 Magnesium (Potential).
FT METAL 143 143 Magnesium (Potential).
FT BINDING 130 130 ATP (By similarity).
FT VARIANT 279 279 E -> D (in dbSNP:rs3800962).
FT /FTId=VAR_050062.
SQ SEQUENCE 318 AA; 34839 MW; 6A4EDC798FB3B296 CRC64;
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIDESVRG EDVYIVQSGC
GEINDSLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRSPISAK LVANMLSIAG
ADHIITMDLH ASQIQGFFDI PVDNLYAEPT VLKWIRENIP EWKNCIIVSP DAGGAKRVTS
IADQLNVDFA LIHKERKKAN EVDCIVLVGD VNDRVAILVD DMADTCVTIC LAADKLLSAG
ATRVYAILTH GIFSGPAISR INTACFEAVV VTNTIPQDEK MKHCSKIRVI DISMILAEAI
RRTHNGESVS YLFSHVPL
//
ID PRPS3_HUMAN Reviewed; 318 AA.
AC P21108; Q6P5P6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 3;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 1-like 1;
DE Short=PRPS1-like 1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase III;
DE Short=PRS-III;
GN Name=PRPS1L1; Synonyms=PRPS3, PRPSL;
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], AND PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Testis;
RX PubMed=2168892;
RA Taira M., Iizasa T., Shimada H., Kudoh J., Shimizu N., Tatibana M.;
RT "A human testis-specific mRNA for phosphoribosylpyrophosphate
RT synthetase that initiates from a non-AUG codon.";
RL J. Biol. Chem. 265:16491-16497(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-279.
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate
CC (PRPP) that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Activated by magnesium and inorganic phosphate.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed
CC of 3 homodimers (By similarity).
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
CC -!- CAUTION: According to PubMed:2168892, this sequence initiates from
CC a non-AUG codon; N-terminal ACG codon did serve as a start codon.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M57423; AAB59463.1; -; mRNA.
DR EMBL; BC062797; AAH62797.2; -; mRNA.
DR PIR; A37893; KIHUR3.
DR RefSeq; NP_787082.1; NM_175886.2.
DR UniGene; Hs.169284; -.
DR ProteinModelPortal; P21108; -.
DR SMR; P21108; 3-313.
DR STRING; 9606.ENSP00000390134; -.
DR PhosphoSite; P21108; -.
DR DMDM; 125585; -.
DR SWISS-2DPAGE; P21108; -.
DR PRIDE; P21108; -.
DR GeneID; 221823; -.
DR KEGG; hsa:221823; -.
DR UCSC; uc003stz.3; human.
DR CTD; 221823; -.
DR GeneCards; GC07M018066; -.
DR H-InvDB; HIX0033604; -.
DR HGNC; HGNC:9463; PRPS1L1.
DR MIM; 611566; gene.
DR neXtProt; NX_P21108; -.
DR PharmGKB; PA33818; -.
DR HOGENOM; HOG000210451; -.
DR HOVERGEN; HBG001520; -.
DR InParanoid; P21108; -.
DR KO; K00948; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00087; UER00172.
DR GenomeRNAi; 221823; -.
DR NextBio; 91465; -.
DR PRO; PR:P21108; -.
DR CleanEx; HS_PRPS1L1; -.
DR Genevestigator; P21108; -.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; ISS:UniProtKB.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; NAS:UniProtKB.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Direct protein sequencing; Kinase;
KW Magnesium; Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW Polymorphism; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 318 Ribose-phosphate pyrophosphokinase 3.
FT /FTId=PRO_0000141078.
FT NP_BIND 96 101 ATP (By similarity).
FT REGION 212 227 Binding of phosphoribosylpyrophosphate
FT (Potential).
FT METAL 128 128 Magnesium (Potential).
FT METAL 130 130 Magnesium (Potential).
FT METAL 139 139 Magnesium (Potential).
FT METAL 143 143 Magnesium (Potential).
FT BINDING 130 130 ATP (By similarity).
FT VARIANT 279 279 E -> D (in dbSNP:rs3800962).
FT /FTId=VAR_050062.
SQ SEQUENCE 318 AA; 34839 MW; 6A4EDC798FB3B296 CRC64;
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIDESVRG EDVYIVQSGC
GEINDSLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRSPISAK LVANMLSIAG
ADHIITMDLH ASQIQGFFDI PVDNLYAEPT VLKWIRENIP EWKNCIIVSP DAGGAKRVTS
IADQLNVDFA LIHKERKKAN EVDCIVLVGD VNDRVAILVD DMADTCVTIC LAADKLLSAG
ATRVYAILTH GIFSGPAISR INTACFEAVV VTNTIPQDEK MKHCSKIRVI DISMILAEAI
RRTHNGESVS YLFSHVPL
//
MIM
611566
*RECORD*
*FIELD* NO
611566
*FIELD* TI
*611566 PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE 1-LIKE 1; PRPS1L1
;;PRPS1-LIKE 1;;
PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE 3; PRPS3
read more*FIELD* TX
CLONING
Using rat Prps1 (311850) to screen a human testis cDNA library, Taira et
al. (1990) cloned PRPS1L1, which they called PRPS3. The deduced
318-amino acid protein has a calculated molecular mass of 34.7 kD.
Peptide sequencing and mutagenesis experiments showed that translation
of PRPS3 initiates at an ACG codon that specifies methionine rather than
threonine, and that this methionine is subsequently removed, resulting
in a mature protein with an N-terminal proline. In vitro transcription
and cell-free translation resulted in a protein with an apparent
molecular mass of 38 kD. Northern blot analysis detected a 1.4-kb
transcript in human testis. Prps3 expression was not detected in testis
of 3-week-old rats, but its expression increased after 4 weeks, roughly
correlating with the appearance of primary spermatocytes.
MAPPING
By Southern blot and somatic cell hybrid analyses, Taira et al. (1990)
mapped the PRPS1L1 gene to chromosome 7.
*FIELD* RF
1. Taira, M.; Iizasa, T.; Shimada, H.; Kudoh, J.; Shimizu, N.; Tatibana,
M.: A human testis-specific mRNA for phosphoribosylpyrophosphate
synthetase that initiates from a non-AUG codon. J. Biol. Chem. 265:
16491-16497, 1990.
*FIELD* CD
Patricia A. Hartz: 10/30/2007
*FIELD* ED
mgross: 10/30/2007
*RECORD*
*FIELD* NO
611566
*FIELD* TI
*611566 PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE 1-LIKE 1; PRPS1L1
;;PRPS1-LIKE 1;;
PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE 3; PRPS3
read more*FIELD* TX
CLONING
Using rat Prps1 (311850) to screen a human testis cDNA library, Taira et
al. (1990) cloned PRPS1L1, which they called PRPS3. The deduced
318-amino acid protein has a calculated molecular mass of 34.7 kD.
Peptide sequencing and mutagenesis experiments showed that translation
of PRPS3 initiates at an ACG codon that specifies methionine rather than
threonine, and that this methionine is subsequently removed, resulting
in a mature protein with an N-terminal proline. In vitro transcription
and cell-free translation resulted in a protein with an apparent
molecular mass of 38 kD. Northern blot analysis detected a 1.4-kb
transcript in human testis. Prps3 expression was not detected in testis
of 3-week-old rats, but its expression increased after 4 weeks, roughly
correlating with the appearance of primary spermatocytes.
MAPPING
By Southern blot and somatic cell hybrid analyses, Taira et al. (1990)
mapped the PRPS1L1 gene to chromosome 7.
*FIELD* RF
1. Taira, M.; Iizasa, T.; Shimada, H.; Kudoh, J.; Shimizu, N.; Tatibana,
M.: A human testis-specific mRNA for phosphoribosylpyrophosphate
synthetase that initiates from a non-AUG codon. J. Biol. Chem. 265:
16491-16497, 1990.
*FIELD* CD
Patricia A. Hartz: 10/30/2007
*FIELD* ED
mgross: 10/30/2007