Q13018 (PLA2R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Secretory phospholipase A2 receptor
Short name=PLA2-R
Short name=PLA2R

Alternative name(s):
180 kDa secretory phospholipase A2 receptor
C-type lectin domain family 13 member C
M-type receptor

Cleaved into the following chain:

1. Soluble secretory phospholipase A2 receptor
   Short name=Soluble PLA2-R
   Short name=Soluble PLA2R

Gene names

Name:	PLA2R1
Synonyms:	CLEC13C

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	1463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phosholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B. Ref.1 Ref.7
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Soluble secretory phospholipase A2 receptor: Secreted By similarity. Isoform 2: Secreted Potential.
Tissue specificity	Present in lung macrophage (at protein level). Highly expressed in kidney. Also expressed in pancreas, amnion, choriodecidua and placenta. Isoform 2 is expressed at much lower level. Ref.1 Ref.5 Ref.6 Ref.7
Domain	C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B. The endocytosis signal probably mediates endocytosis via clathrin-coated pits By similarity.
Post-translational modification	The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments, or by alternative splicing, as in the case of isoform 2 that shares all characteristics of secretory phospholipase A2 receptor form By similarity.
Sequence similarities	Contains 8 C-type lectin domains. Contains 1 fibronectin type-II domain. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Lectin
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokine production Inferred from mutant phenotype Ref.7. Source: UniProtKB negative regulation of arachidonic acid secretion Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of phospholipase A2 activity Inferred from sequence or structural similarity. Source: UniProtKB oxidative stress-induced premature senescence Inferred from mutant phenotype PubMed 19197340. Source: UniProtKB positive regulation of DNA damage response, signal transduction by p53 class mediator Inferred from mutant phenotype PubMed 19197340. Source: UniProtKB positive regulation of arachidonic acid secretion Inferred from sequence or structural similarity. Source: UniProtKB reactive oxygen species metabolic process Inferred from direct assay PubMed 19197340. Source: UniProtKB receptor-mediated endocytosis Inferred from direct assay Ref.1. Source: UniProtKB replicative senescence Inferred from mutant phenotype PubMed 19197340. Source: UniProtKB
Cellular_component	cell surface Inferred from direct assay Ref.7. Source: UniProtKB extracellular region Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Non-traceable author statement Ref.1. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 12225974. Source: UniProtKB
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro receptor activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13018-1)

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: Q13018-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1323-1324: NE → SK
     1325-1463: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	By similarity
	Chain	21 – 1463	1443	Secretory phospholipase A2 receptor		PRO_5000144349
	Chain	21 – ?		Soluble secretory phospholipase A2 receptor By similarity		PRO_0000311250
Regions
	Topological domain	21 – 1397	1377	Extracellular Potential
	Transmembrane	1398 – 1418	21	Helical; Potential
	Topological domain	1419 – 1463	45	Cytoplasmic Potential
	Domain	38 – 161	124	Ricin B-type lectin
	Domain	173 – 221	49	Fibronectin type-II
	Domain	238 – 355	118	C-type lectin 1
	Domain	385 – 502	118	C-type lectin 2
	Domain	522 – 643	122	C-type lectin 3
	Domain	673 – 797	125	C-type lectin 4
	Domain	819 – 938	120	C-type lectin 5
	Domain	965 – 1096	132	C-type lectin 6
	Domain	1121 – 1232	112	C-type lectin 7
	Domain	1257 – 1378	122	C-type lectin 8
	Motif	1436 – 1442	7	Endocytosis signal
Amino acid modifications
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Glycosylation	454	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 64		By similarity
	Disulfide bond	89 ↔ 106		By similarity
	Disulfide bond	178 ↔ 204		By similarity
	Disulfide bond	192 ↔ 219		By similarity
	Disulfide bond	260 ↔ 354		By similarity
	Disulfide bond	330 ↔ 346		By similarity
	Disulfide bond	406 ↔ 501		By similarity
	Disulfide bond	478 ↔ 493		By similarity
	Disulfide bond	617 ↔ 634		By similarity
	Disulfide bond	699 ↔ 796		By similarity
	Disulfide bond	774 ↔ 788		By similarity
	Disulfide bond	840 ↔ 937		By similarity
	Disulfide bond	914 ↔ 929		By similarity
	Disulfide bond	1067 ↔ 1087		By similarity
	Disulfide bond	1209 ↔ 1223		By similarity
	Disulfide bond	1280 ↔ 1377		By similarity
	Disulfide bond	1354 ↔ 1369		By similarity
Natural variations
	Alternative sequence	1323 – 1324	2	NE → SK in isoform 2.		VSP_029493
	Alternative sequence	1325 – 1463	139	Missing in isoform 2.		VSP_029494
	Natural variant	142	1	R → Q. Corresponds to variant rs12327936 [ dbSNP | Ensembl ].		VAR_037203
	Natural variant	177	1	P → S. Corresponds to variant rs13394676 [ dbSNP | Ensembl ].		VAR_037204
	Natural variant	279	1	I → V. Corresponds to variant rs965290 [ dbSNP | Ensembl ].		VAR_037205
	Natural variant	292	1	M → V. Ref.1 Corresponds to variant rs3749117 [ dbSNP | Ensembl ].		VAR_037206
	Natural variant	300	1	H → D. Ref.1 Corresponds to variant rs35771982 [ dbSNP | Ensembl ].		VAR_037207
	Natural variant	370	1	A → E. Corresponds to variant rs34916310 [ dbSNP | Ensembl ].		VAR_061354
	Natural variant	404	1	R → H. Corresponds to variant rs33985939 [ dbSNP | Ensembl ].		VAR_037208
	Natural variant	1106	1	G → S. Corresponds to variant rs3828323 [ dbSNP | Ensembl ].		VAR_037209
Experimental info
	Sequence conflict	15 – 17	3	APR → GAA in AAA70110. Ref.1
	Sequence conflict	15 – 17	3	APR → GAA in AAC50163. Ref.1
	Sequence conflict	62 – 64	3	ENC → GRTGS in AAA70110. Ref.1
	Sequence conflict	62 – 64	3	ENC → GRTGS in AAC50163. Ref.1
	Sequence conflict	521 – 523	3	RHG → ETC in AAA70110. Ref.1
	Sequence conflict	521 – 523	3	RHG → ETC in AAC50163. Ref.1
	Sequence conflict	724	1	S → P in AAA70110. Ref.1
	Sequence conflict	724	1	S → P in AAC50163. Ref.1
	Sequence conflict	779	1	A → P in AAA70110. Ref.1
	Sequence conflict	779	1	A → P in AAC50163. Ref.1
	Sequence conflict	1224	1	E → D in AAA70110. Ref.1
	Sequence conflict	1224	1	E → D in AAC50163. Ref.1
	Sequence conflict	1263	1	S → K in AAA70110. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 4E65EA5AC5D597E2	FASTA	1,463	168,600
	10 20 30 40 50 60 MLLSPSLLLL LLLGAPRGCA EGVAAALTPE RLLEWQDKGI FVIQSESLKK CIQAGKSVLT 70 80 90 100 110 120 LENCKQANKH MLWKWVSNHG LFNIGGSGCL GLNFSAPEQP LSLYECDSTL VSLRWRCNRK 130 140 150 160 170 180 MITGPLQYSV QVAHDNTVVA SRKYIHKWIS YGSGGGDICE YLHKDLHTIK GNTHGMPCMF 190 200 210 220 230 240 PFQYNHQWHH ECTREGREDD LLWCATTSRY ERDEKWGFCP DPTSAEVGCD TIWEKDLNSH 250 260 270 280 290 300 ICYQFNLLSS LSWSEAHSSC QMQGGTLLSI TDETEENFIR EHMSSKTVEV WMGLNQLDEH 310 320 330 340 350 360 AGWQWSDGTP LNYLNWSPEV NFEPFVEDHC GTFSSFMPSA WRSRDCESTL PYICKKYLNH 370 380 390 400 410 420 IDHEIVEKDA WKYYATHCEP GWNPYNRNCY KLQKEEKTWH EALRSCQADN SALIDITSLA 430 440 450 460 470 480 EVEFLVTLLG DENASETWIG LSSNKIPVSF EWSNDSSVIF TNWHTLEPHI FPNRSQLCVS 490 500 510 520 530 540 AEQSEGHWKV KNCEERLFYI CKKAGHVLSD AESGCQEGWE RHGGFCYKID TVLRSFDQAS 550 560 570 580 590 600 SGYYCPPALV TITNRFEQAF ITSLISSVVK MKDSYFWIAL QDQNDTGEYT WKPVGQKPEP 610 620 630 640 650 660 VQYTHWNTHQ PRYSGGCVAM RGRHPLGRWE VKHCRHFKAM SLCKQPVENQ EKAEYEERWP 670 680 690 700 710 720 FHPCYLDWES EPGLASCFKV FHSEKVLMKR TWREAEAFCE EFGAHLASFA HIEEENFVNE 730 740 750 760 770 780 LLHSKFNWTE ERQFWIGFNK RNPLNAGSWE WSDRTPVVSS FLDNTYFGED ARNCAVYKAN 790 800 810 820 830 840 KTLLPLHCGS KREWICKIPR DVKPKIPFWY QYDVPWLFYQ DAEYLFHTFA SEWLNFEFVC 850 860 870 880 890 900 SWLHSDLLTI HSAHEQEFIH SKIKALSKYG ASWWIGLQEE RANDEFRWRD GTPVIYQNWD 910 920 930 940 950 960 TGRERTVNNQ SQRCGFISSI TGLWGSEECS VSMPSICKRK KVWLIEKKKD TPKQHGTCPK 970 980 990 1000 1010 1020 GWLYFNYKCL LLNIPKDPSS WKNWTHAQHF CAEEGGTLVA IESEVEQAFI TMNLFGQTTS 1030 1040 1050 1060 1070 1080 VWIGLQNDDY ETWLNGKPVV YSNWSPFDII NIPSHNTTEV QKHIPLCALL SSNPNFHFTG 1090 1100 1110 1120 1130 1140 KWYFEDCGKE GYGFVCEKMQ DTSGHGVNTS DMYPMPNTLE YGNRTYKIIN ANMTWYAAIK 1150 1160 1170 1180 1190 1200 TCLMHKAQLV SITDQYHQSF LTVVLNRLGY AHWIGLFTTD NGLNFDWSDG TKSSFTFWKD 1210 1220 1230 1240 1250 1260 EESSLLGDCV FADSNGRWHS TACESFLQGA ICHVPPETRQ SEHPELCSET SIPWIKFKSN 1270 1280 1290 1300 1310 1320 CYSFSTVLDS MSFEAAHEFC KKEGSNLLTI KDEAENAFLL EELFAFGSSV QMVWLNAQFD 1330 1340 1350 1360 1370 1380 GNNETIKWFD GTPTDQSNWG IRKPDTDYFK PHHCVALRIP EGLWQLSPCQ EKKGFICKME 1390 1400 1410 1420 1430 1440 ADIHTAEALP EKGPSHSIIP LAVVLTLIVI VAICTLSFCI YKHNGGFFRR LAGFRNPYYP 1450 1460 ATNFSTVYLE ENILISDLEK SDQ
	Isoform 2 [UniParc]. Checksum: E00D5FDFF05DC9FC	FASTA	1,324	152,805
	10 20 30 40 50 60 MLLSPSLLLL LLLGAPRGCA EGVAAALTPE RLLEWQDKGI FVIQSESLKK CIQAGKSVLT 70 80 90 100 110 120 LENCKQANKH MLWKWVSNHG LFNIGGSGCL GLNFSAPEQP LSLYECDSTL VSLRWRCNRK 130 140 150 160 170 180 MITGPLQYSV QVAHDNTVVA SRKYIHKWIS YGSGGGDICE YLHKDLHTIK GNTHGMPCMF 190 200 210 220 230 240 PFQYNHQWHH ECTREGREDD LLWCATTSRY ERDEKWGFCP DPTSAEVGCD TIWEKDLNSH 250 260 270 280 290 300 ICYQFNLLSS LSWSEAHSSC QMQGGTLLSI TDETEENFIR EHMSSKTVEV WMGLNQLDEH 310 320 330 340 350 360 AGWQWSDGTP LNYLNWSPEV NFEPFVEDHC GTFSSFMPSA WRSRDCESTL PYICKKYLNH 370 380 390 400 410 420 IDHEIVEKDA WKYYATHCEP GWNPYNRNCY KLQKEEKTWH EALRSCQADN SALIDITSLA 430 440 450 460 470 480 EVEFLVTLLG DENASETWIG LSSNKIPVSF EWSNDSSVIF TNWHTLEPHI FPNRSQLCVS 490 500 510 520 530 540 AEQSEGHWKV KNCEERLFYI CKKAGHVLSD AESGCQEGWE RHGGFCYKID TVLRSFDQAS 550 560 570 580 590 600 SGYYCPPALV TITNRFEQAF ITSLISSVVK MKDSYFWIAL QDQNDTGEYT WKPVGQKPEP 610 620 630 640 650 660 VQYTHWNTHQ PRYSGGCVAM RGRHPLGRWE VKHCRHFKAM SLCKQPVENQ EKAEYEERWP 670 680 690 700 710 720 FHPCYLDWES EPGLASCFKV FHSEKVLMKR TWREAEAFCE EFGAHLASFA HIEEENFVNE 730 740 750 760 770 780 LLHSKFNWTE ERQFWIGFNK RNPLNAGSWE WSDRTPVVSS FLDNTYFGED ARNCAVYKAN 790 800 810 820 830 840 KTLLPLHCGS KREWICKIPR DVKPKIPFWY QYDVPWLFYQ DAEYLFHTFA SEWLNFEFVC 850 860 870 880 890 900 SWLHSDLLTI HSAHEQEFIH SKIKALSKYG ASWWIGLQEE RANDEFRWRD GTPVIYQNWD 910 920 930 940 950 960 TGRERTVNNQ SQRCGFISSI TGLWGSEECS VSMPSICKRK KVWLIEKKKD TPKQHGTCPK 970 980 990 1000 1010 1020 GWLYFNYKCL LLNIPKDPSS WKNWTHAQHF CAEEGGTLVA IESEVEQAFI TMNLFGQTTS 1030 1040 1050 1060 1070 1080 VWIGLQNDDY ETWLNGKPVV YSNWSPFDII NIPSHNTTEV QKHIPLCALL SSNPNFHFTG 1090 1100 1110 1120 1130 1140 KWYFEDCGKE GYGFVCEKMQ DTSGHGVNTS DMYPMPNTLE YGNRTYKIIN ANMTWYAAIK 1150 1160 1170 1180 1190 1200 TCLMHKAQLV SITDQYHQSF LTVVLNRLGY AHWIGLFTTD NGLNFDWSDG TKSSFTFWKD 1210 1220 1230 1240 1250 1260 EESSLLGDCV FADSNGRWHS TACESFLQGA ICHVPPETRQ SEHPELCSET SIPWIKFKSN 1270 1280 1290 1300 1310 1320 CYSFSTVLDS MSFEAAHEFC KKEGSNLLTI KDEAENAFLL EELFAFGSSV QMVWLNAQFD GNSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization." Ancian P., Lambeau G., Mattei M.-G., Lazdunski M. J. Biol. Chem. 270:8963-8970(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANTS VAL-292 AND ASP-300. Tissue: Kidney.
[2]	"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].
[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] (ISOFORM 1). Tissue: Brain.
[5]	"Structural comparison of phospholipase-A2-binding regions in phospholipase-A2 receptors from various mammals." Higashino K., Ishizaki J., Kishino J., Ohara O., Arita H. Eur. J. Biochem. 225:375-382(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 532-942, TISSUE SPECIFICITY. Tissue: Placenta.
[6]	"Distribution of the phospholipase A2 receptor messenger RNA in human gestational tissues." Moses E.K., Freed K.A., Brennecke S.P., Rice G.E. Placenta 19:35-40(1998) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Activation of cytokine production by secreted phospholipase A2 in human lung macrophages expressing the M-type receptor." Granata F., Petraroli A., Boilard E., Bezzine S., Bollinger J., Del Vecchio L., Gelb M.H., Lambeau G., Marone G., Triggiani M. J. Immunol. 174:464-474(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Phospholipase A2 receptor

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17033 mRNA. Translation: AAA70110.1. U17034 mRNA. Translation: AAC50163.1. AC080166 Genomic DNA. Translation: AAY24052.1. AC093873 Genomic DNA. Translation: AAY24190.1. CH471058 Genomic DNA. Translation: EAX11392.1. CH471058 Genomic DNA. Translation: EAX11393.1. BC140823 mRNA. Translation: AAI40824.1. D30780 mRNA. Translation: BAA06444.1.
IPI	IPI00105353. IPI00480099.
PIR	A56395. B56395.
RefSeq	NP_001007268.1. NM_001007267.2. NP_001182570.1. NM_001195641.1. NP_031392.3. NM_007366.4.
UniGene	Hs.410477.
3D structure databases
HSSP	HSSP built from PDB template 1CXW based on UniProtKB P08253.
ProteinModelPortal	Q13018.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000283243.
Polymorphism databases
DMDM	160419241.
Proteomic databases
PaxDb	Q13018.
PRIDE	Q13018.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000283243; ENSP00000283243; ENSG00000153246. ENST00000392771; ENSP00000376524; ENSG00000153246.
GeneID	22925.
KEGG	hsa:22925.
UCSC	uc002ube.2. human. uc002ubf.3. human.
Organism-specific databases
CTD	22925.
GeneCards	GC02M160788.
H-InvDB	HIX0024010.
HGNC	HGNC:9042. PLA2R1.
HPA	HPA012657.
MIM	604939. gene.
neXtProt	NX_Q13018.
PharmGKB	PA33369.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG288621.
HOVERGEN	HBG108261.
InParanoid	Q13018.
KO	K06560.
OMA	GNRTYKI.
OrthoDB	EOG4ZGPBJ.
PhylomeDB	Q13018.
Gene expression databases
Bgee	Q13018.
CleanEx	HS_PLA2R1.
Genevestigator	Q13018.
Family and domain databases
Gene3D	2.10.10.10. 1 hit. 3.10.100.10. 8 hits.
InterPro	IPR001304. C-type_lectin. IPR016186. C-type_lectin-like. IPR018378. C-type_lectin_CS. IPR016187. C-type_lectin_fold. IPR000562. FN_type2_col-bd. IPR013806. Kringle-like. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF00040. fn2. 1 hit. PF00059. Lectin_C. 8 hits. [Graphical view]
SMART	SM00034. CLECT. 8 hits. SM00059. FN2. 1 hit. SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF56436. C-type_lectin_fold. 8 hits. SSF57440. Kringle-like. 1 hit. SSF50370. RicinB_like. 1 hit.
PROSITE	PS00615. C_TYPE_LECTIN_1. 3 hits. PS50041. C_TYPE_LECTIN_2. 8 hits. PS00023. FN2_1. 1 hit. PS51092. FN2_2. 1 hit. PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PLA2R1. human.
GenomeRNAi	22925.
NextBio	43633.
SOURCE	Search...

Entry information

Entry name

PLA2R_HUMAN

Accession

Primary (citable) accession number: Q13018
Secondary accession number(s): B2RTU9 , D3DPB1, Q13019, Q15095, Q53R45, Q53RR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 102 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.