Q14642 (I5P1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type I inositol 1,4,5-trisphosphate 5-phosphatase
Short name=5PTase
EC=3.1.3.56

Gene names

Name:

INPP5A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction.
Catalytic activity	D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
Subcellular location	Membrane; Lipid-anchor.
Tissue specificity	Brain; high level in Purkinje cells.
Sequence similarities	Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type I family.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase
PTM	Lipoprotein Methylation Palmitate Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell communication Non-traceable author statement. Source: UniProtKB phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane Non-traceable author statement Ref.5. Source: UniProtKB
Molecular_function	inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-1,4,5-trisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-polyphosphate 5-phosphatase activity Non-traceable author statement Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 409	409	Type I inositol 1,4,5-trisphosphate 5-phosphatase		PRO_0000209719
	Propeptide	410 – 412	3	Removed in mature form Potential		PRO_0000396780
Amino acid modifications
	Modified residue	409	1	Cysteine methyl ester Potential
	Lipidation	408	1	S-palmitoyl cysteine Potential
	Lipidation	409	1	S-farnesyl cysteine Potential
Natural variations
	Natural variant	45	1	K → R. Corresponds to variant rs1133400 [ dbSNP | Ensembl ].		VAR_034006
Experimental info
	Sequence conflict	152 – 172	21	PQDYF…RTRWC → RRLLPRVQMVKKRLHPDEVV in CAA83500. Ref.5
	Sequence conflict	247 – 251	5	CTKAT → SAKPP in CAA83500. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q14642 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F55C0DFDDA01A850	FASTA	412	47,820
	10 20 30 40 50 60 MAGKAAAPGT AVLLVTANVG SLFDDPENLQ KNWLREFYQV VHTHKPHFMA LHCQEFGGKN 70 80 90 100 110 120 YEASMSHVDK FVKELLSSDA MKEYNRARVY LDENYKSQEH FTALGSFYFL HESLKNIYQF 130 140 150 160 170 180 DFKAKKYRKV AGKEIYSDTL ESTPMLEKEK FPQDYFPECK WSRKGFIRTR WCIADCAFDL 190 200 210 220 230 240 VNIHLFHDAS NLVAWETSPS VYSGIRHKAL GYVLDRIIDQ RFEKVSYFVF GDFNFRLDSK 250 260 270 280 290 300 SVVETLCTKA TMQTVRAADT NEVVKLIFRE SDNDRKVMLQ LEKKLFDYFN QEVFRDNNGT 310 320 330 340 350 360 ALLEFDKELS VFKDRLYELD ISFPPSYPYS EDARQGEQYM NTRCPAWCDR ILMSPSAKEL 370 380 390 400 410 VLRSESEEKV VTYDHIGPNV CMGDHKPVFL AFRIMPGAGK PHAHVHKCCV VQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells." de Smedt F., Verjans B., Mailleux P., Erneux C. FEBS Lett. 347:69-72(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase." Laxminarayan K.M., Chan B.K., Tetaz T., Bird P.I., Mitchell C.A. J. Biol. Chem. 269:17305-17310(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-412. Tissue: Placenta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77567 mRNA. Translation: CAA54676.1. AL392043, AL356603, AL451069 Genomic DNA. Translation: CAI39945.1. AL451069, AL392043, AL356603 Genomic DNA. Translation: CAI14121.1. AL356603, AL451069, AL392043 Genomic DNA. Translation: CAI40942.1. CH471211 Genomic DNA. Translation: EAW61306.1. CH471211 Genomic DNA. Translation: EAW61307.1. BC096280 mRNA. Translation: AAH96280.1. Z31695 mRNA. Translation: CAA83500.1.
IPI	IPI00032262.
PIR	S45721.
RefSeq	NP_005530.3. NM_005539.3.
UniGene	Hs.523360. Hs.715308.
3D structure databases
ProteinModelPortal	Q14642.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000357583.
PTM databases
PhosphoSite	Q14642.
Polymorphism databases
DMDM	3122245.
Proteomic databases
PaxDb	Q14642.
PRIDE	Q14642.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368594; ENSP00000357583; ENSG00000068383.
GeneID	3632.
KEGG	hsa:3632.
UCSC	uc001llp.3. human.
Organism-specific databases
CTD	3632.
GeneCards	GC10P134351.
HGNC	HGNC:6076. INPP5A.
HPA	HPA012285.
MIM	600106. gene.
neXtProt	NX_Q14642.
PharmGKB	PA29884.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG288675.
HOGENOM	HOG000006583.
HOVERGEN	HBG006102.
InParanoid	Q14642.
KO	K01106.
OMA	RQYMNTR.
OrthoDB	EOG49P9ZD.
Enzyme and pathway databases
BioCyc	MetaCyc:HS00936-MONOMER.
BRENDA	3.1.3.56. 2681.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q14642.
Bgee	Q14642.
CleanEx	HS_INPP5A.
Genevestigator	Q14642.
GermOnline	ENSG00000068383. Homo sapiens.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. [Graphical view]
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SMART	SM00128. IPPc. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
ProtoNet	Search...
Other
BindingDB	Q14642.
ChEMBL	CHEMBL4243.
GenomeRNAi	3632.
NextBio	14213.
SOURCE	Search...

Entry information

Entry name

I5P1_HUMAN

Accession

Primary (citable) accession number: Q14642
Secondary accession number(s): D3DXI3, Q14640, Q5JSF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.