P05455 (LA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lupus La protein

Alternative name(s):
La autoantigen
La ribonucleoprotein
Sjoegren syndrome type B antigen
Short name=SS-B

Gene names

Name:

SSB

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	408 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to the 3' poly(U) terminii of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. Ref.2 Ref.10
Subunit structure	Interacts with DDX15. May interact with RUFY1. Ref.12 Ref.13
Subcellular location	Nucleus Probable.
Post-translational modification	Phosphorylated. The phosphorylation sites are at the C-terminal part of the protein. Ref.11 The N-terminus is blocked.
Miscellaneous	Sera from patients with systemic lupus erythematosus (SLE) often contain antibodies that react with the normal cellular La protein as if this antigen was foreign.
Sequence similarities	Contains 1 HTH La-type RNA-binding domain. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Systemic lupus erythematosus
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone mRNA metabolic process Traceable author statement PubMed 9154801. Source: ProtInc tRNA modification Traceable author statement PubMed 10983981. Source: ProtInc
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Traceable author statement Ref.2. Source: ProtInc
Molecular_function	mRNA binding Traceable author statement PubMed 9154801. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro tRNA binding Traceable author statement PubMed 10983981. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 408

408

Lupus La protein

PRO_0000207599

Regions

Domain

7 – 99

93

HTH La-type RNA-binding

Domain

111 – 187

77

RRM

Amino acid modifications

Modified residue

116

1

N6-acetyllysine Ref.19

Modified residue

128

1

N6-acetyllysine Ref.19

Modified residue

328

1

N6-acetyllysine Ref.19

Modified residue

360

1

N6-acetyllysine Ref.19

Modified residue

366

1

Phosphoserine; by CK2 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.22

Natural variations

Natural variant

48

1

P → S.
Corresponds to variant rs17160793 [ dbSNP | Ensembl ].

VAR_034066

Experimental info

Sequence conflict

54

1

K → E in AAA36577. Ref.8

Secondary structure

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408

Helix Strand Turn

Details...

Helix

11 – 24

14

Turn

27 – 29

3

Helix

30 – 32

3

Helix

34 – 42

9

Turn

43 – 45

3

Beta strand

46 – 48

3

Helix

49 – 52

4

Helix

56 – 61

6

Helix

65 – 73

9

Beta strand

80 – 82

3

Beta strand

86 – 91

6

Helix

102 – 110

9

Beta strand

112 – 116

5

Helix

124 – 131

8

Helix

132 – 134

3

Beta strand

137 – 144

8

Beta strand

146 – 148

3

Beta strand

150 – 160

11

Helix

161 – 169

9

Beta strand

174 – 177

4

Beta strand

181 – 184

4

Turn

185 – 187

3

Beta strand

233 – 239

7

Helix

246 – 252

7

Beta strand

259 – 263

5

Beta strand

269 – 277

9

Helix

279 – 288

10

Turn

289 – 291

3

Beta strand

298 – 304

7

Helix

308 – 326

19

Sequences

	Sequence		Length	Mass (Da)
	P05455 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: EC153C15F9187FC4	FASTA	408	46,837
	10 20 30 40 50 60 MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE IMIKFNRLNR 70 80 90 100 110 120 LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV TDEYKNDVKN RSVYIKGFPT 130 140 150 160 170 180 DATLDDIKEW LEDKGQVLNI QMRRTLHKAF KGSIFVVFDS IESAKKFVET PGQKYKETDL 190 200 210 220 230 240 LILFKDDYFA KKNEERKQNK VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL 250 260 270 280 290 300 DDQTCREDLH ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE 310 320 330 340 350 360 VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS GKGKVQFQGK 370 380 390 400 KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK TENGAGDQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ribonucleoprotein SS-B/La belongs to a protein family with consensus sequences for RNA-binding." Chan E.K.L., Sullivan K.F., Tan E.M. Nucleic Acids Res. 17:2233-2244(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic structure and amino acid sequence domains of the human La autoantigen." Chambers J.C., Kenan D., Martin B.J., Keene J.D. J. Biol. Chem. 263:18043-18051(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ROLE IN LUPUS ERYTHEMATOSUS.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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]. Tissue: Placenta and Skeletal muscle.
[8]	"Characteristics and epitope mapping of a cloned human autoantigen La." Sturgess A.D., Peterson M.G., McNeilage L.J., Whittingham S., Coppel R.S. J. Immunol. 140:3212-3218(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-408.
[9]	"Isolation and analysis of cDNA clones expressing human lupus La antigen." Chambers J.C., Keene J.D. Proc. Natl. Acad. Sci. U.S.A. 82:2115-2119(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-97.
[10]	"Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III." Gottlieb E., Steitz J.A. EMBO J. 8:851-861(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes." Fan H., Sakulich A.L., Goodier J.L., Zhang X., Qin J., Maraie R.J. Cell 88:707-715(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-366.
[12]	"The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a putative DEAH-box RNA helicase." Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S., Van Venrooij W.J., Pruijn G.J.M. RNA 8:1428-1443(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX15.
[13]	"Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes." Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J., van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M. Mol. Biol. Cell 15:611-624(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RUFY1.
[14]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Liver.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-328 AND LYS-360, MASS SPECTROMETRY.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY.
[23]	"Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element." Jacks A., Babon J., Kelly G., Manolaridis I., Cary P.D., Curry S., Conte M.R. Structure 11:833-843(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 225-334.
[24]	"Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein." Alfano C., Sanfelice D., Babon J., Kelly G., Jacks A., Curry S., Conte M.R. Nat. Struct. Mol. Biol. 11:323-329(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-202.
[25]	"Structural basis for recognition and sequestration of UUU(OH) 3' termini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen." Teplova M., Yuan Y.R., Phan A.T., Malinina L., Ilin S., Teplov A., Patel D.J. Mol. Cell 21:75-85(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-194.
[26]	"Structural analysis reveals conformational plasticity in the recognition of RNA 3' ends by the human La protein." Kotik-Kogan O., Valentine E.R., Sanfelice D., Conte M.R., Curry S. Structure 16:852-862(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-194.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X13697 mRNA. Translation: CAA31985.1.
J04205 mRNA. Translation: AAA51885.1.
BT009862 mRNA. Translation: AAP88864.1.
AB451228 mRNA. Translation: BAG70042.1.
AC009967 Genomic DNA. Translation: AAY14868.1.
CH471058 Genomic DNA. Translation: EAX11258.1.
CH471058 Genomic DNA. Translation: EAX11259.1.
BC001289 mRNA. Translation: AAH01289.1.
BC020818 mRNA. Translation: AAH20818.1.
M20328 mRNA. Translation: AAA36577.1.

IPI

IPI00009032.

PIR

A31888.

RefSeq

NP_003133.1. NM_003142.4.

UniGene

Hs.632535.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OWX	NMR	-	A	225-334	[»]
1S79	NMR	-	A	105-202	[»]
1S7A	NMR	-	A	1-103	[»]
1YTY	X-ray	2.29	A/B	1-194	[»]
1ZH5	X-ray	1.85	A/B	1-194	[»]
2VOD	X-ray	2.10	A/B	4-194	[»]
2VON	X-ray	2.10	A/B	4-194	[»]
2VOO	X-ray	1.80	A/B	4-194	[»]
2VOP	X-ray	2.80	A	4-194	[»]

DisProt

DP00229.

ProteinModelPortal

P05455.

SMR

P05455. Positions 10-188, 225-334.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29750N.

IntAct

P05455. 19 interactions.

MINT

MINT-5002383.

STRING

9606.ENSP00000260956.

PTM databases

PhosphoSite

P05455.

Polymorphism databases

DMDM

125985.

Proteomic databases

PaxDb

P05455.

PeptideAtlas

P05455.

PRIDE

P05455.

Protocols and materials databases

DNASU

6741.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260956; ENSP00000260956; ENSG00000138385.
ENST00000409333; ENSP00000386636; ENSG00000138385.

GeneID

6741.

KEGG

hsa:6741.

UCSC

uc002ufk.3. human.

Organism-specific databases

CTD

6741.

GeneCards

GC02P170619.

HGNC

HGNC:11316. SSB.

HPA

CAB004643.
HPA012385.
HPA017287.

MIM

109090. gene.

neXtProt

NX_P05455.

PharmGKB

PA36140.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5193.

HOGENOM

HOG000006947.

HOVERGEN

HBG001407.

InParanoid

P05455.

KO

K11090.

OMA

ENAEMKS.

OrthoDB

EOG4C2HB3.

PhylomeDB

P05455.

Gene expression databases

ArrayExpress

P05455.

Bgee

P05455.

CleanEx

HS_SSB.

Genevestigator

P05455.

GermOnline

ENSG00000138385. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
3.30.70.330. 2 hits.

InterPro

IPR002344. Lupus_La.
IPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR014886. RRM_3.
IPR000504. RRM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF05383. La. 1 hit.
PF00076. RRM_1. 1 hit.
PF08777. RRM_3. 1 hit.
[Graphical view]

PRINTS

PR00302. LUPUSLA.

SMART

SM00715. LA. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50961. HTH_LA. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P05455.

GenomeRNAi

6741.

NextBio

26296.

PMAP-CutDB

P05455.

SOURCE

Search...

Entry information

Entry name

LA_HUMAN

Accession

Primary (citable) accession number: P05455
Secondary accession number(s): Q15367, Q53XJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 163 of the entry and version 2 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.