Q62028 (PLA2R_MOUSE) 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
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:	Pla2g1br

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1487 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 phosholipases sPLA2-IB/PLA2G1B, sPLA2-X/PLA2G10 and, with lower affinity, 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 and sPLA2-X/PLA2G10. Ref.1 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subcellular location	Cell membrane; Single-pass type I membrane protein Ref.12. Soluble secretory phospholipase A2 receptor: Secreted Ref.12.
Tissue specificity	Widely expressed. Present in type II alveolar epithelial cells and a subset of splenic lymphocytes. Present at the surface of polymorphonuclear neutrophils (at protein level). Ref.1 Ref.5 Ref.11
Induction	Following exposure to endotoxin (at protein level). Ref.5
Domain	C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B. Ref.1 The endocytosis signal probably mediates endocytosis via clathrin-coated pits By similarity. Ref.1
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 reported by Ref.12, or by alternative splicing.
Disruption phenotype	Mice are viable, fertile and without evident histopathological abnormalities. After challenge with bacterial lipopolysaccharide (LPS), they exhibit longer survival than wild-type mice. They are also resistant to lethal effects of exogenous sPLA2-IB/PLA2G1B after sensitization with sublethal dose of LPS, suggesting a potential role in the progression of endotoxic shock. Ref.4
Sequence similarities	Contains 8 C-type lectin domains. Contains 1 fibronectin type-II domain. Contains 1 ricin B-type lectin domain.
Sequence caution	The sequence CAM22305.1 differs from that shown. Reason: Erroneous initiation. The sequence CAM23630.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing
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 sequence or structural similarity. Source: UniProtKB negative regulation of arachidonic acid secretion Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of phospholipase A2 activity Inferred from direct assay Ref.12. Source: UniProtKB oxidative stress-induced premature senescence Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of DNA damage response, signal transduction by p53 class mediator Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of arachidonic acid secretion Inferred from direct assay Ref.8. Source: UniProtKB reactive oxygen species metabolic process Inferred from sequence or structural similarity. Source: UniProtKB receptor-mediated endocytosis Inferred from direct assay Ref.1. Source: UniProtKB replicative senescence Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara extracellular region Inferred from direct assay Ref.12. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q62028-1)

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: Q62028-2)

The sequence of this isoform differs from the canonical sequence as follows:
     680-689: VFHSEKVLMK → DTGKAVLDWI
     690-1487: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	By similarity
	Chain	27 – 1487	1461	Secretory phospholipase A2 receptor		PRO_5000139804
	Chain	27 – ?		Soluble secretory phospholipase A2 receptor Probable		PRO_0000311251
Regions
	Topological domain	27 – 1396	1370	Extracellular Potential
	Transmembrane	1397 – 1417	21	Helical; Potential
	Topological domain	1418 – 1487	70	Cytoplasmic Potential
	Domain	42 – 165	124	Ricin B-type lectin
	Domain	176 – 224	49	Fibronectin type-II
	Domain	241 – 357	117	C-type lectin 1
	Domain	387 – 504	118	C-type lectin 2
	Domain	524 – 643	120	C-type lectin 3
	Domain	673 – 797	125	C-type lectin 4
	Domain	819 – 938	120	C-type lectin 5
	Domain	964 – 1095	132	C-type lectin 6
	Domain	1120 – 1231	112	C-type lectin 7
	Domain	1256 – 1377	122	C-type lectin 8
	Motif	1435 – 1441	7	Endocytosis signal
Amino acid modifications
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	239	1	N-linked (GlcNAc...) Potential
	Glycosylation	928	1	N-linked (GlcNAc...) Potential
	Glycosylation	1107	1	N-linked (GlcNAc...) Potential
	Glycosylation	1122	1	N-linked (GlcNAc...) Potential
	Glycosylation	1131	1	N-linked (GlcNAc...) Potential
	Disulfide bond	55 ↔ 68		By similarity
	Disulfide bond	93 ↔ 110		By similarity
	Disulfide bond	181 ↔ 207		By similarity
	Disulfide bond	195 ↔ 222		By similarity
	Disulfide bond	263 ↔ 356		By similarity
	Disulfide bond	333 ↔ 348		By similarity
	Disulfide bond	408 ↔ 503		By similarity
	Disulfide bond	480 ↔ 495		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	1066 ↔ 1086		By similarity
	Disulfide bond	1208 ↔ 1222		By similarity
	Disulfide bond	1279 ↔ 1376		By similarity
	Disulfide bond	1353 ↔ 1368		By similarity
Natural variations
	Alternative sequence	680 – 689	10	VFHSEKVLMK → DTGKAVLDWI in isoform 2.		VSP_029495
	Alternative sequence	690 – 1487	798	Missing in isoform 2.		VSP_029496

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: AD8D905859B0EDE8	FASTA	1,487	170,512
	10 20 30 40 50 60 MVQWLAMLQL LWLQQLLLLG IHQGIAQDLT HIQEPSLEWR DKGIFIIQSE SLKTCIQAGK 70 80 90 100 110 120 SVLTLENCKQ PNEHMLWKWV SDDHLFNVGG SGCLGLNISA LEQPLKLYEC DSTLISLRWH 130 140 150 160 170 180 CDRKMIEGPL QYKVQVKSDN TVVARKQIHR WIAYTSSGGD ICEHPSRDLY TLKGNAHGMP 190 200 210 220 230 240 CVFPFQFKGH WHHDCIREGQ KEHLLWCATT SRYEEDEKWG FCPDPTSMKV FCDATWQRNG 250 260 270 280 290 300 SSRICYQFNL LSSLSWNQAH SSCLMQGGAL LSIADEDEED FIRKHLSKVV KEVWIGLNQL 310 320 330 340 350 360 DEKAGWQWSD GTPLSYLNWS QEITPGPFVE HHCGTLEVVS AAWRSRDCES TLPYICKRDL 370 380 390 400 410 420 NHTAQGILEK DSWKYHATHC DPDWTPFNRK CYKLKKDRKS WLGALHSCQS NDSVLMDVAS 430 440 450 460 470 480 LAEVEFLVSL LRDENASETW IGLSSNKIPV SFEWSSGSSV IFTNWYPLEP RILPNRRQLC 490 500 510 520 530 540 VSAEESDGRW KVKDCKERLF YICKKAGQVP ADEQSGCPAG WERHGRFCYK IDTVLRSFEE 550 560 570 580 590 600 ASSGYYCSPA LLTITSRFEQ AFITSLISSV AEKDSYFWIA LQDQNNTGEY TWKTVGQREP 610 620 630 640 650 660 VQYTYWNTRQ PSNRGGCVVV RGGSSLGRWE VKDCSDFKAM SLCKTPVKIW EKTELEERWP 670 680 690 700 710 720 FHPCYMDWES ATGLASCFKV FHSEKVLMKR SWREAEAFCE EFGAHLASFA HIEEENFVNE 730 740 750 760 770 780 LLHSKFNWTQ ERQFWIGFNR RNPLNAGSWA WSDGSPVVSS FLDNAYFEED AKNCAVYKAN 790 800 810 820 830 840 KTLLPSNCAS KHEWICRIPR DVRPKFPDWY QYDAPWLFYQ NAEYLFHTHP AEWATFEFVC 850 860 870 880 890 900 GWLRSDFLTI YSAQEQEFIH SKIKGLTKYG VKWWIGLEEG GARDQIQWSN GSPVIFQNWD 910 920 930 940 950 960 KGREERVDSQ RKRCVFISSI TGLWGTENCS VPLPSICKRV KIWVIEKEKP PTQPGTCPKG 970 980 990 1000 1010 1020 WLYFNYKCFL VTIPKDPREL KTWTGAQEFC VAKGGTLVSI KSELEQAFIT MNLFGQTTNV 1030 1040 1050 1060 1070 1080 WIGLQSTNHE KWVNGKPLVY SNWSPSDIIN IPSYNTTEFQ KHIPLCALMS SNPNFHFTGK 1090 1100 1110 1120 1130 1140 WYFDDCGKEG YGFVCEKMQD TLEHHVNVSD TSAIPSTLEY GNRTYKIIRG NMTWYAAGKS 1150 1160 1170 1180 1190 1200 CRMHRAELAS IPDAFHQAFL TVLLSRLGHT HWIGLSTTDN GQTFDWSDGT KSPFTYWKDE 1210 1220 1230 1240 1250 1260 ESAFLGDCAF ADTNGRWHST ACESFLQGAI CHVVTETKAF EHPGLCSETS VPWIKFKGNC 1270 1280 1290 1300 1310 1320 YSFSTVLDSR SFEDAHEFCK SEGSNLLAIR DAAENSFLLE ELLAFGSSVQ MVWLNAQFDN 1330 1340 1350 1360 1370 1380 NNKTLRWFDG TPTEQSNWGL RKPDMDHLKP HPCVVLRIPE GIWHFTPCED KKGFICKMEA 1390 1400 1410 1420 1430 1440 GIPAVTAQPE KGLSHSIVPV TVTLTLIIAL GIFMLCFWIY KQKSDIFQRL TGSRGSYYPT 1450 1460 1470 1480 LNFSTAHLEE NILISDLEKN TNDEEVRDAP ATESKRGHKG RPICISP
	Isoform 2 [UniParc]. Checksum: 846ED8D4A79573B4	FASTA	689	79,127
	10 20 30 40 50 60 MVQWLAMLQL LWLQQLLLLG IHQGIAQDLT HIQEPSLEWR DKGIFIIQSE SLKTCIQAGK 70 80 90 100 110 120 SVLTLENCKQ PNEHMLWKWV SDDHLFNVGG SGCLGLNISA LEQPLKLYEC DSTLISLRWH 130 140 150 160 170 180 CDRKMIEGPL QYKVQVKSDN TVVARKQIHR WIAYTSSGGD ICEHPSRDLY TLKGNAHGMP 190 200 210 220 230 240 CVFPFQFKGH WHHDCIREGQ KEHLLWCATT SRYEEDEKWG FCPDPTSMKV FCDATWQRNG 250 260 270 280 290 300 SSRICYQFNL LSSLSWNQAH SSCLMQGGAL LSIADEDEED FIRKHLSKVV KEVWIGLNQL 310 320 330 340 350 360 DEKAGWQWSD GTPLSYLNWS QEITPGPFVE HHCGTLEVVS AAWRSRDCES TLPYICKRDL 370 380 390 400 410 420 NHTAQGILEK DSWKYHATHC DPDWTPFNRK CYKLKKDRKS WLGALHSCQS NDSVLMDVAS 430 440 450 460 470 480 LAEVEFLVSL LRDENASETW IGLSSNKIPV SFEWSSGSSV IFTNWYPLEP RILPNRRQLC 490 500 510 520 530 540 VSAEESDGRW KVKDCKERLF YICKKAGQVP ADEQSGCPAG WERHGRFCYK IDTVLRSFEE 550 560 570 580 590 600 ASSGYYCSPA LLTITSRFEQ AFITSLISSV AEKDSYFWIA LQDQNNTGEY TWKTVGQREP 610 620 630 640 650 660 VQYTYWNTRQ PSNRGGCVVV RGGSSLGRWE VKDCSDFKAM SLCKTPVKIW EKTELEERWP 670 680 FHPCYMDWES ATGLASCFKD TGKAVLDWI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 1), FUNCTION, DOMAIN, TISSUE SPECIFICITY.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"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] (ISOFORMS 1 AND 2). Tissue: Brain and Eye.
[4]	"Resistance to endotoxic shock in phospholipase A2 receptor-deficient mice." Hanasaki K., Yokota Y., Ishizaki J., Itoh T., Arita H. J. Biol. Chem. 272:32792-32797(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"Enhanced tissue expression and elevated circulating level of phospholipase A(2) receptor during murine endotoxic shock." Yokota Y., Ikeda M., Higashino K., Nakano K., Fujii N., Arita H., Hanasaki K. Arch. Biochem. Biophys. 379:7-17(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]	"Mouse group X secretory phospholipase A2 induces a potent release of arachidonic acid from spleen cells and acts as a ligand for the phospholipase A2 receptor." Morioka Y., Saiga A., Yokota Y., Suzuki N., Ikeda M., Ono T., Nakano K., Fujii N., Ishizaki J., Arita H., Hanasaki K. Arch. Biochem. Biophys. 381:31-42(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Identification of group X secretory phospholipase A(2) as a natural ligand for mouse phospholipase A(2) receptor." Yokota Y., Higashino K., Nakano K., Arita H., Hanasaki K. FEBS Lett. 478:187-191(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Secretory phospholipase A2 receptor-mediated activation of cytosolic phospholipase A2 in murine bone marrow-derived mast cells." Fonteh A.N., Atsumi G., LaPorte T., Chilton F.H. J. Immunol. 165:2773-2782(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Pancreatic phospholipase A2 via its receptor regulates expression of key enzymes of phospholipid and sphingolipid metabolism." Mandal A.K., Zhang Z., Chou J.Y., Mukherjee A.B. FASEB J. 15:1834-1836(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Clearance of group X secretory phospholipase A(2) via mouse phospholipase A(2) receptor." Yokota Y., Notoya M., Higashino K., Ishimoto Y., Nakano K., Arita H., Hanasaki K. FEBS Lett. 509:250-254(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Presence of the M-type sPLA(2) receptor on neutrophils and its role in elastase release and adhesion." Silliman C.C., Moore E.E., Zallen G., Gonzalez R., Johnson J.L., Elzi D.J., Meng X., Hanasaki K., Ishizaki J., Arita H., Ao L., England K.M., Banerjee A. Am. J. Physiol. 283:C1102-C1113(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]	"Identification of a soluble form phospholipase A2 receptor as a circulating endogenous inhibitor for secretory phospholipase A2." Higashino Ki K., Yokota Y., Ono T., Kamitani S., Arita H., Hanasaki K. J. Biol. Chem. 277:13583-13588(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, POSSIBLE PROTEOLYTIC PROCESSING.
[13]	"Binding to the high-affinity M-type receptor for secreted phospholipases A(2) is not obligatory for the presynaptic neurotoxicity of ammodytoxin A." Prijatelj P., Vardjan N., Rowan E.G., Krizaj I., Pungercar J. Biochimie 88:1425-1433(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Recombinant production and properties of binding of the full set of mouse secreted phospholipases A2 to the mouse M-type receptor." Rouault M., Le Calvez C., Boilard E., Surrel F., Singer A., Ghomashchi F., Bezzine S., Scarzello S., Bollinger J., Gelb M.H., Lambeau G. Biochemistry 46:1647-1662(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Phospholipase A2 receptor

Cross-references

Sequence databases
EMBL GenBank DDBJ	D30779 mRNA. Translation: BAA06443.1. BX679662, AL928546 Genomic DNA. Translation: CAM22305.1. Different initiation. AL928546, BX679662 Genomic DNA. Translation: CAM23630.1. Different initiation. BC048780 mRNA. Translation: AAH48780.1. BC141355 mRNA. Translation: AAI41356.1. BC141356 mRNA. Translation: AAI41357.1.
IPI	IPI00120953. IPI00988318.
PIR	S48719.
RefSeq	NP_032893.1. NM_008867.2.
UniGene	Mm.5092.
3D structure databases
HSSP	HSSP built from PDB template 1J7M based on UniProtKB P08253.
ProteinModelPortal	Q62028.
SMR	Q62028. Positions 120-358, 380-505, 517-613, 664-798, 816-1096, 1253-1379.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000108144.
Proteomic databases
PaxDb	Q62028.
PRIDE	Q62028.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067708; ENSMUSP00000065205; ENSMUSG00000054580. ENSMUST00000112525; ENSMUSP00000108144; ENSMUSG00000054580.
GeneID	18779.
KEGG	mmu:18779.
UCSC	uc008jug.1. mouse. uc008juh.1. mouse.
Organism-specific databases
CTD	22925.
MGI	MGI:102468. Pla2r1.
Phylogenomic databases
eggNOG	NOG288621.
GeneTree	ENSGT00700000104195.
HOGENOM	HOG000231191.
HOVERGEN	HBG108261.
InParanoid	Q62028.
KO	K06560.
OrthoDB	EOG4ZGPBJ.
Gene expression databases
Bgee	Q62028.
CleanEx	MM_PLA2R1.
Genevestigator	Q62028.
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. 2 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
NextBio	295027.
SOURCE	Search...

Entry information

Entry name

PLA2R_MOUSE

Accession

Primary (citable) accession number: Q62028
Secondary accession number(s): A2AS64, B9EJ68, Q80ZL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program