Q15735 (PI5PA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
EC=3.1.3.56

Alternative name(s):
Inositol polyphosphate 5-phosphatase J

Gene names

Name:	INPP5J
Synonyms:	PIB5PA, PIPP

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	1006 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles By similarity.
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	Cytoplasm By similarity. Note: Predominantly localized to membrane ruffles By similarity.
Domain	The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein.
Sequence similarities	Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type II family.
Sequence caution	The sequence AAD15618.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of microtubule polymerization Inferred from electronic annotation. Source: Compara negative regulation of neuron projection development Inferred from electronic annotation. Source: Compara negative regulation of peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome dendritic shaft Inferred from electronic annotation. Source: Compara growth cone Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara ruffle Inferred from direct assay PubMed 12536145. Source: MGI
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 Inferred from electronic annotation. Source: EC phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15735-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15735-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-367: Missing.

Isoform 3 (identifier: Q15735-3)

The sequence of this isoform differs from the canonical sequence as follows:
     56-423: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1006	1006	Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A		PRO_0000209738
Regions
	Region	425 – 728	304	Catalytic Potential
	Region	729 – 840	112	Required for ruffle localization By similarity
	Motif	102 – 107	6	RSXSXX motif 1
	Motif	345 – 350	6	SH3-binding Potential
	Motif	350 – 355	6	RSXSXX motif 2
	Motif	874 – 879	6	RSXSXX motif 3
	Motif	885 – 890	6	RSXSXX motif 4
	Motif	911 – 916	6	RSXSXX motif 5
	Compositional bias	122 – 371	250	Pro-rich
	Compositional bias	840 – 937	98	Ser-rich
Amino acid modifications
	Modified residue	347	1	Phosphoserine By similarity
	Modified residue	349	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 367	367	Missing in isoform 2.		VSP_007296
	Alternative sequence	56 – 423	368	Missing in isoform 3.		VSP_021017
	Natural variant	333	1	S → I. Corresponds to variant rs12485025 [ dbSNP | Ensembl ].		VAR_028107
Experimental info
	Sequence conflict	610 – 612	3	SYD → ARG Ref.5
	Sequence conflict	662	1	V → A in BAC86611. Ref.1
	Sequence conflict	791	1	W → R in AAI09289. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: ADB6382AA33E15AC	FASTA	1,006	107,197
	10 20 30 40 50 60 MEGQSSRGSR RPGTRAGLGS LPMPQGVAQT GAPSKVDSSF QLPAKKNAAL GPSEPRLALA 70 80 90 100 110 120 PVGPRAAMSA SSEGPRLALA SPRPILAPLC TPEGQKTATA HRSSSLAPTS VGQLVMSASA 130 140 150 160 170 180 GPKPPPATTG SVLAPTSLGL VMPASAGPRS PPVTLGPNLA PTSRDQKQEP PASVGPKPTL 190 200 210 220 230 240 AASGLSLALA SEEQPPELPS TPSPVPSPVL SPTQEQALAP ASTASGAASV GQTSARKRDA 250 260 270 280 290 300 PAPRPLPASE GHLQPPAQTS GPTGSPPCIQ TSPDPRLSPS FRARPEALHS SPEDPVLPRP 310 320 330 340 350 360 PQTLPLDVGQ GPSEPGTHSP GLLSPTFRPG APSGQTVPPP LPKPPRSPSR SPSHSPNRSP 370 380 390 400 410 420 CVPPAPDMAL PRLGTQSTGP GRCLSPNLQA QEAPAPVTTS SSTSTLSSSP WSAQPTWKSD 430 440 450 460 470 480 PGFRITVVTW NVGTAMPPDD VTSLLHLGGG DDSDGADMIA IGLQEVNSML NKRLKDALFT 490 500 510 520 530 540 DQWSELFMDA LGPFNFVLVS SVRMQGVILL LFAKYYHLPF LRDVQTDCTR TGLGGYWGNK 550 560 570 580 590 600 GGVSVRLAAF GHMLCFLNCH LPAHMDKAEQ RKDNFQTILS LQQFQGPGAQ GILDHDLVFW 610 620 630 640 650 660 FGDLNFRIES YDLHFVKFAI DSDQLHQLWE KDQLNMAKNT WPILKGFQEG PLNFAPTFKF 670 680 690 700 710 720 DVGTNKYDTS AKKRKPAWTD RILWKVKAPG GGPSPSGRKS HRLQVTQHSY RSHMEYTVSD 730 740 750 760 770 780 HKPVAAQFLL QFAFRDDMPL VRLEVADEWV RPEQAVVRYR METVFARSSW DWIGLYRVGF 790 800 810 820 830 840 RHCKDYVAYV WAKHEDVDGN TYQVTFSEES LPKGHGDFIL GYYSHNHSIL IGITEPFQIS 850 860 870 880 890 900 LPSSELASSS TDSSGTSSEG EDDSTLELLA PKSRSPSPGK SKRHRSRSPG LARFPGLALR 910 920 930 940 950 960 PSSRERRGAS RSPSPQSRRL SRVAPDRSSN GSSRGSSEEG PSGLPGPWAF PPAVPRSLGL 970 980 990 1000 LPALRLETVD PGGGGSWGPD REALAPNSLS PSPQGHRGLE EGGLGP
	Isoform 2 [UniParc]. Checksum: 3ED5CD8BBB3398D0	FASTA	639	70,464
	10 20 30 40 50 60 MALPRLGTQS TGPGRCLSPN LQAQEAPAPV TTSSSTSTLS SSPWSAQPTW KSDPGFRITV 70 80 90 100 110 120 VTWNVGTAMP PDDVTSLLHL GGGDDSDGAD MIAIGLQEVN SMLNKRLKDA LFTDQWSELF 130 140 150 160 170 180 MDALGPFNFV LVSSVRMQGV ILLLFAKYYH LPFLRDVQTD CTRTGLGGYW GNKGGVSVRL 190 200 210 220 230 240 AAFGHMLCFL NCHLPAHMDK AEQRKDNFQT ILSLQQFQGP GAQGILDHDL VFWFGDLNFR 250 260 270 280 290 300 IESYDLHFVK FAIDSDQLHQ LWEKDQLNMA KNTWPILKGF QEGPLNFAPT FKFDVGTNKY 310 320 330 340 350 360 DTSAKKRKPA WTDRILWKVK APGGGPSPSG RKSHRLQVTQ HSYRSHMEYT VSDHKPVAAQ 370 380 390 400 410 420 FLLQFAFRDD MPLVRLEVAD EWVRPEQAVV RYRMETVFAR SSWDWIGLYR VGFRHCKDYV 430 440 450 460 470 480 AYVWAKHEDV DGNTYQVTFS EESLPKGHGD FILGYYSHNH SILIGITEPF QISLPSSELA 490 500 510 520 530 540 SSSTDSSGTS SEGEDDSTLE LLAPKSRSPS PGKSKRHRSR SPGLARFPGL ALRPSSRERR 550 560 570 580 590 600 GASRSPSPQS RRLSRVAPDR SSNGSSRGSS EEGPSGLPGP WAFPPAVPRS LGLLPALRLE 610 620 630 TVDPGGGGSW GPDREALAPN SLSPSPQGHR GLEEGGLGP
	Isoform 3 [UniParc]. Checksum: 3F8ECF77ECC71C26	FASTA	638	70,239
	10 20 30 40 50 60 MEGQSSRGSR RPGTRAGLGS LPMPQGVAQT GAPSKVDSSF QLPAKKNAAL GPSEPRITVV 70 80 90 100 110 120 TWNVGTAMPP DDVTSLLHLG GGDDSDGADM IAIGLQEVNS MLNKRLKDAL FTDQWSELFM 130 140 150 160 170 180 DALGPFNFVL VSSVRMQGVI LLLFAKYYHL PFLRDVQTDC TRTGLGGYWG NKGGVSVRLA 190 200 210 220 230 240 AFGHMLCFLN CHLPAHMDKA EQRKDNFQTI LSLQQFQGPG AQGILDHDLV FWFGDLNFRI 250 260 270 280 290 300 ESYDLHFVKF AIDSDQLHQL WEKDQLNMAK NTWPILKGFQ EGPLNFAPTF KFDVGTNKYD 310 320 330 340 350 360 TSAKKRKPAW TDRILWKVKA PGGGPSPSGR KSHRLQVTQH SYRSHMEYTV SDHKPVAAQF 370 380 390 400 410 420 LLQFAFRDDM PLVRLEVADE WVRPEQAVVR YRMETVFARS SWDWIGLYRV GFRHCKDYVA 430 440 450 460 470 480 YVWAKHEDVD GNTYQVTFSE ESLPKGHGDF ILGYYSHNHS ILIGITEPFQ ISLPSSELAS 490 500 510 520 530 540 SSTDSSGTSS EGEDDSTLEL LAPKSRSPSP GKSKRHRSRS PGLARFPGLA LRPSSRERRG 550 560 570 580 590 600 ASRSPSPQSR RLSRVAPDRS SNGSSRGSSE EGPSGLPGPW AFPPAVPRSL GLLPALRLET 610 620 630 VDPGGGGSWG PDREALAPNS LSPSPQGHRG LEEGGLGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Cerebellum, Heart and Spleen.
[2]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
[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 (JUL-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] (ISOFORM 2).
[5]	Nussbaum R.L. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 610-1006. Tissue: Brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK092859 mRNA. Translation: BAG52616.1. AK095944 mRNA. Translation: BAC04657.1. AK126610 mRNA. Translation: BAC86611.1. AC005005 Genomic DNA. Translation: AAD15618.1. Sequence problems. CH471095 Genomic DNA. Translation: EAW59936.1. BC109288 mRNA. Translation: AAI09289.1. U45975 mRNA. Translation: AAB03216.1.
IPI	IPI00242711. IPI00242712. IPI00445092.
RefSeq	NP_001002837.1. NM_001002837.1.
UniGene	Hs.517549.
3D structure databases
ProteinModelPortal	Q15735.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000384534.
PTM databases
PhosphoSite	Q15735.
Polymorphism databases
DMDM	116242713.
Proteomic databases
PaxDb	Q15735.
PRIDE	Q15735.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331075; ENSP00000333262; ENSG00000185133. ENST00000400294; ENSP00000383150; ENSG00000185133. ENST00000404390; ENSP00000384534; ENSG00000185133. ENST00000405300; ENSP00000384596; ENSG00000185133.
GeneID	27124.
KEGG	hsa:27124.
UCSC	uc003ajs.4. human. uc003ajt.4. human.
Organism-specific databases
CTD	27124.
GeneCards	GC22P031518.
HGNC	HGNC:8956. INPP5J.
HPA	HPA034539.
MIM	606481. gene.
neXtProt	NX_Q15735.
PharmGKB	PA164720918.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5411.
HOGENOM	HOG000046051.
HOVERGEN	HBG082135.
InParanoid	Q15735.
KO	K01106.
OMA	APTSVGQ.
OrthoDB	EOG4HDSTN.
PhylomeDB	Q15735.
Enzyme and pathway databases
BioCyc	MetaCyc:HS11950-MONOMER.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q15735.
Bgee	Q15735.
CleanEx	HS_INPP5J.
Genevestigator	Q15735.
GermOnline	ENSG00000185133. 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
GenomeRNAi	27124.
NextBio	49824.
SOURCE	Search...

Entry information

Entry name

PI5PA_HUMAN

Accession

Primary (citable) accession number: Q15735
Secondary accession number(s): B3KS54 , Q32M61, Q6ZTH6, Q8N902, Q9UDT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 112 of the entry and version 3 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.