Q91VN0 (LRP5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low-density lipoprotein receptor-related protein 5
Short name=LRP-5

Alternative name(s):
Low-density lipoprotein receptor-related protein 7
Short name=LRP-7
Lr3

Gene names

Name:	Lrp5
Synonyms:	Lrp7

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	1614 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	Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin By similarity. Appears be required for postnatal control of vascular regression in the eye. Required for posterior patterning of the epiblast during gastrulation. Ref.5 Ref.7
Subunit structure	Homodimer; disulfide-linked. Forms phosphorylated oligomer aggregates on Wnt-signaling. Component of a WNT-signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts with FZD8; the interaction is formed on WNT-binding and signaling. Interacts (via the phosphorylated PPPSP motif domains) with AXIN1; the interaction prevents inhibition of beta-catenin phosphorylation and signaling and is enhanced in the presence of GSK3B and WNT1 or WNT3A. Interacts (via beta-propeller regions 3 and 4) with DKK1; the interaction, enhanced by MESD and/or KREMEN, inhibits beta-catenin signaling by preventing GSK3-mediated phosphorylation of the PPPSP motifs and subsequent, AXIN1 binding. Interacts with CSNK1E. Interacts with SOST; the interaction antagonizes canonical Wnt signaling. Interacts with APCDD1 By similarity. Interacts with MESD; the interaction prevents the formation of LRP5 aggregates, targets LRP5 to the plasma membrane and, when complexed with KREMEN2, increases DKK1 binding. Ref.6
Subcellular location	Membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Note: Chaperoned to the plasma membrane by MESD By similarity. Ref.6
Tissue specificity	Widely expressed, with the highest expression levels in liver, heart, and lung and the lowest levels in brain and spleen. Expressed in early embryo with strongest expression in visceral endoderm overlying the extraembryonic ectoderm. Not present in the mesoderm nor in endoderm emerging from the primitive streak. Ref.7
Developmental stage	Expressed before or on embryonic day 7.
Post-translational modification	Phosphorylation of cytoplasmic PPPSP motifs regulates the signal transduction of the Wnt signaling pathway through acting as a docking site for AXIN1 By similarity.
Disruption phenotype	Mice exhibit decreased osteoblast proliferation, developing low bone mass postnatally. Also display persistent embryonic eye vascularization due to a failure of macrophage-induced endothelial cell apoptosis. LRP5 null mutants exhibit a loss of middle phalanx ossification at 18.5 dpc. Double null LRP5/LRP6 mutants are more severely affected. Embryos arrest prior to mid-gestation. Ref.5 Ref.7
Sequence similarities	Belongs to the LDLR family. Contains 4 EGF-like domains. Contains 3 LDL-receptor class A domains. Contains 20 LDL-receptor class B repeats.

Ontologies

Keywords
Biological process	Endocytosis Wnt signaling pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway involved in dorsal/ventral axis specification Inferred from Biological aspect of Ancestor. Source: RefGenome adipose tissue development Inferred from Biological aspect of Ancestor. Source: RefGenome anatomical structure regression Inferred from mutant phenotype PubMed 16163358. Source: MGI anterior/posterior pattern specification Inferred from genetic interaction Ref.7. Source: MGI bone marrow development Inferred from Biological aspect of Ancestor. Source: RefGenome bone morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome bone remodeling Inferred from mutant phenotype Ref.5PubMed 15207752PubMed 16790443PubMed 17147489PubMed 17627087. Source: MGI branching involved in mammary gland duct morphogenesis Inferred from mutant phenotype PubMed 16973609. Source: MGI canonical Wnt receptor signaling pathway Inferred from direct assay PubMed 15035989. Source: BHF-UCL cell migration involved in gastrulation Inferred from genetic interaction Ref.7. Source: MGI cell-cell signaling involved in mammary gland development Inferred from mutant phenotype PubMed 16973609. Source: MGI cholesterol homeostasis Inferred from Biological aspect of Ancestor. Source: RefGenome cholesterol metabolic process Inferred from mutant phenotype PubMed 12509515. Source: MGI embryonic camera-type eye morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome embryonic digit morphogenesis Inferred from genetic interaction Ref.7. Source: MGI embryonic retina morphogenesis in camera-type eye Inferred from Biological aspect of Ancestor. Source: RefGenome endocytosis Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix-cell signaling Inferred from direct assay PubMed 15035989. Source: BHF-UCL gastrulation with mouth forming second Inferred from genetic interaction Ref.7. Source: MGI induction of apoptosis Inferred from mutant phenotype PubMed 16163358. Source: MGI osteoblast development Inferred from mutant phenotype PubMed 17700537. Source: BHF-UCL positive regulation of osteoblast proliferation Inferred from mutant phenotype Ref.5. Source: MGI positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 15035989. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of bone remodeling Inferred from mutant phenotype PubMed 12817748. Source: MGI regulation of fat cell differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of insulin secretion involved in cellular response to glucose stimulus Inferred from mutant phenotype PubMed 12509515. Source: MGI regulation of ossification Inferred from Biological aspect of Ancestor. Source: RefGenome response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara retinal blood vessel morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome somatic stem cell maintenance Inferred from mutant phenotype PubMed 19672307. Source: MGI
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome receptor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	Wnt-activated receptor activity Inferred from direct assay Ref.5. Source: MGI coreceptor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced.

Isoform 1 (identifier: Q91VN0-1)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Potential
	Chain	31 – 1614	1584	Low-density lipoprotein receptor-related protein 5		PRO_0000017329
Regions
	Topological domain	31 – 1383	1353	Extracellular Potential
	Transmembrane	1384 – 1406	23	Helical; Potential
	Topological domain	1407 – 1614	208	Cytoplasmic Potential
	Repeat	74 – 118	45	LDL-receptor class B 1
	Repeat	119 – 161	43	LDL-receptor class B 2
	Repeat	162 – 205	44	LDL-receptor class B 3
	Repeat	206 – 246	41	LDL-receptor class B 4
	Repeat	247 – 289	43	LDL-receptor class B 5
	Domain	294 – 336	43	EGF-like 1
	Repeat	384 – 426	43	LDL-receptor class B 6
	Repeat	427 – 469	43	LDL-receptor class B 7
	Repeat	470 – 513	44	LDL-receptor class B 8
	Repeat	514 – 556	43	LDL-receptor class B 9
	Repeat	557 – 599	43	LDL-receptor class B 10
	Domain	600 – 640	41	EGF-like 2
	Repeat	686 – 728	43	LDL-receptor class B 11
	Repeat	729 – 771	43	LDL-receptor class B 12
	Repeat	772 – 814	43	LDL-receptor class B 13
	Repeat	815 – 854	40	LDL-receptor class B 14
	Repeat	855 – 897	43	LDL-receptor class B 15
	Domain	901 – 941	41	EGF-like 3
	Repeat	988 – 1034	47	LDL-receptor class B 16
	Repeat	1035 – 1077	43	LDL-receptor class B 17
	Repeat	1078 – 1122	45	LDL-receptor class B 18
	Repeat	1123 – 1164	42	LDL-receptor class B 19
	Repeat	1165 – 1206	42	LDL-receptor class B 20
	Domain	1212 – 1253	42	EGF-like 4
	Domain	1257 – 1295	39	LDL-receptor class A 1
	Domain	1296 – 1332	37	LDL-receptor class A 2
	Domain	1334 – 1370	37	LDL-receptor class A 3
	Region	31 – 287	257	Beta-propeller 1
	Region	340 – 601	262	Beta-propeller 2
	Region	643 – 902	260	Beta-propeller 3
	Region	944 – 1211	268	Beta-propeller 4
	Motif	1499 – 1505	7	PPPSP motif A
	Motif	1537 – 1544	8	PPPSP motif B
	Motif	1573 – 1580	8	PPPSP motif C
	Motif	1590 – 1595	6	PPPSP motif D
	Motif	1604 – 1611	8	PPPSP motif E
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	137	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Glycosylation	498	1	N-linked (GlcNAc...) Potential
	Glycosylation	704	1	N-linked (GlcNAc...) Potential
	Glycosylation	877	1	N-linked (GlcNAc...) Potential
	Disulfide bond	298 ↔ 309		By similarity
	Disulfide bond	305 ↔ 320		By similarity
	Disulfide bond	322 ↔ 335		By similarity
	Disulfide bond	604 ↔ 615		By similarity
	Disulfide bond	611 ↔ 624		By similarity
	Disulfide bond	626 ↔ 639		By similarity
	Disulfide bond	905 ↔ 916		By similarity
	Disulfide bond	912 ↔ 925		By similarity
	Disulfide bond	927 ↔ 940		By similarity
	Disulfide bond	1216 ↔ 1227		By similarity
	Disulfide bond	1223 ↔ 1237		By similarity
	Disulfide bond	1239 ↔ 1252		By similarity
	Disulfide bond	1258 ↔ 1272		By similarity
	Disulfide bond	1265 ↔ 1285		By similarity
	Disulfide bond	1279 ↔ 1294		By similarity
	Disulfide bond	1297 ↔ 1309		By similarity
	Disulfide bond	1304 ↔ 1322		By similarity
	Disulfide bond	1316 ↔ 1331		By similarity
	Disulfide bond	1335 ↔ 1347		By similarity
	Disulfide bond	1342 ↔ 1360		By similarity
	Disulfide bond	1354 ↔ 1369		By similarity
Experimental info
	Sequence conflict	220	1	R → H in AAC70183. Ref.2
	Sequence conflict	1520	1	I → S in AAH11374. Ref.4
	Sequence conflict	1553	1	T → I in AAC36468. Ref.1
	Sequence conflict	1553	1	T → I in AAC70183. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 80FF4288470A4FC5	FASTA	1,614	178,885
	10 20 30 40 50 60 METAPTRAPP PPPPPLLLLV LYCSLVPAAA SPLLLFANRR DVRLVDAGGV KLESTIVASG 70 80 90 100 110 120 LEDAAAVDFQ FSKGAVYWTD VSEEAIKQTY LNQTGAAAQN IVISGLVSPD GLACDWVGKK 130 140 150 160 170 180 LYWTDSETNR IEVANLNGTS RKVLFWQDLD QPRAIALDPA HGYMYWTDWG EAPRIERAGM 190 200 210 220 230 240 DGSTRKIIVD SDIYWPNGLT IDLEEQKLYW ADAKLSFIHR ANLDGSFRQK VVEGSLTHPF 250 260 270 280 290 300 ALTLSGDTLY WTDWQTRSIH ACNKWTGEQR KEILSALYSP MDIQVLSQER QPPFHTPCEE 310 320 330 340 350 360 DNGGCSHLCL LSPREPFYSC ACPTGVQLQD NGKTCKTGAE EVLLLARRTD LRRISLDTPD 370 380 390 400 410 420 FTDIVLQVGD IRHAIAIDYD PLEGYVYWTD DEVRAIRRAY LDGSGAQTLV NTEINDPDGI 430 440 450 460 470 480 AVDWVARNLY WTDTGTDRIE VTRLNGTSRK ILVSEDLDEP RAIVLHPVMG LMYWTDWGEN 490 500 510 520 530 540 PKIECANLDG RDRHVLVNTS LGWPNGLALD LQEGKLYWGD AKTDKIEVIN IDGTKRKTLL 550 560 570 580 590 600 EDKLPHIFGF TLLGDFIYWT DWQRRSIERV HKVKASRDVI IDQLPDLMGL KAVNVAKVVG 610 620 630 640 650 660 TNPCADGNGG CSHLCFFTPR ATKCGCPIGL ELLSDMKTCI IPEAFLVFTS RATIHRISLE 670 680 690 700 710 720 TNNNDVAIPL TGVKEASALD FDVSNNHIYW TDVSLKTISR AFMNGSSVEH VIEFGLDYPE 730 740 750 760 770 780 GMAVDWMGKN LYWADTGTNR IEVARLDGQF RQVLVWRDLD NPRSLALDPT KGYIYWTEWG 790 800 810 820 830 840 GKPRIVRAFM DGTNCMTLVD KVGRANDLTI DYADQRLYWT DLDTNMIESS NMLGQERMVI 850 860 870 880 890 900 ADDLPYPFGL TQYSDYIYWT DWNLHSIERA DKTSGRNRTL IQGHLDFVMD ILVFHSSRQD 910 920 930 940 950 960 GLNDCVHSNG QCGQLCLAIP GGHRCGCASH YTLDPSSRNC SPPSTFLLFS QKFAISRMIP 970 980 990 1000 1010 1020 DDQLSPDLVL PLHGLRNVKA INYDPLDKFI YWVDGRQNIK RAKDDGTQPS MLTSPSQSLS 1030 1040 1050 1060 1070 1080 PDRQPHDLSI DIYSRTLFWT CEATNTINVH RLDGDAMGVV LRGDRDKPRA IAVNAERGYM 1090 1100 1110 1120 1130 1140 YFTNMQDHAA KIERASLDGT EREVLFTTGL IRPVALVVDN ALGKLFWVDA DLKRIESCDL 1150 1160 1170 1180 1190 1200 SGANRLTLED ANIVQPVGLT VLGRHLYWID RQQQMIERVE KTTGDKRTRV QGRVTHLTGI 1210 1220 1230 1240 1250 1260 HAVEEVSLEE FSAHPCARDN GGCSHICIAK GDGTPRCSCP VHLVLLQNLL TCGEPPTCSP 1270 1280 1290 1300 1310 1320 DQFACTTGEI DCIPGAWRCD GFPECADQSD EEGCPVCSAS QFPCARGQCV DLRLRCDGEA 1330 1340 1350 1360 1370 1380 DCQDRSDEAN CDAVCLPNQF RCTSGQCVLI KQQCDSFPDC ADGSDELMCE INKPPSDDIP 1390 1400 1410 1420 1430 1440 AHSSAIGPVI GIILSLFVMG GVYFVCQRVM CQRYTGASGP FPHEYVGGAP HVPLNFIAPG 1450 1460 1470 1480 1490 1500 GSQHGPFPGI PCSKSVMSSM SLVGGRGSVP LYDRNHVTGA SSSSSSSTKA TLYPPILNPP 1510 1520 1530 1540 1550 1560 PSPATDPSLY NVDVFYSSGI PATARPYRPY VIRGMAPPTT PCSTDVCDSD YSTSRWKSSK 1570 1580 1590 1600 1610 YYLDLNSDSD PYPPPPTPHS QYLSAEDSCP PSPGTERSYC HLFPPPPSPC TDSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a novel member of the low-density lipoprotein receptor family." Hey P.J., Twells R.C.J., Phillips M.S., Nakagawa Y., Brown S.D., Kawaguchi Y., Cox R., Xie G., Dugan V., Hammond H., Metzker M.L., Todd J.A., Hess J.F. Gene 216:103-111(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Molecular cloning of mouse Lrp7(Lr3) cDNA and chromosomal mapping of orthologous genes in mouse and human." Chen D., Lathrop W., Dong Y. Genomics 55:314-321(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING. Tissue: Liver.
[3]	"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.
[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: Mammary tumor.
[5]	"Cbfa1-independent decrease in osteoblast proliferation, osteopenia, and persistent embryonic eye vascularization in mice deficient in Lrp5, a Wnt coreceptor." Kato M., Patel M.S., Levasseur R., Lobov I., Chang B.H., Glass D.A. II, Hartmann C., Li L., Hwang T.H., Brayton C.F., Lang R.A., Karsenty G., Chan L. J. Cell Biol. 157:303-314(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[6]	"Mesd encodes an LRP5/6 chaperone essential for specification of mouse embryonic polarity." Hsieh J.-C., Lee L., Zhang L., Wefer S., Brown K., DeRossi C., Wines M.E., Rosenquist T., Holdener B.C. Cell 112:355-367(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MESD, OLIGOMERIZATION, SUBCELLULAR LOCATION.
[7]	"The Wnt co-receptors Lrp5 and Lrp6 are essential for gastrulation in mice." Kelly O.G., Pinson K.I., Skarnes W.C. Development 131:2803-2815(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF064984 mRNA. Translation: AAC36468.1. AF077847 mRNA. Translation: AAC70183.1. AC112990 Genomic DNA. No translation available. AC117797 Genomic DNA. No translation available. BC011374 mRNA. Translation: AAH11374.1.
IPI	IPI00135406.
RefSeq	NP_032539.2. NM_008513.3.
UniGene	Mm.274581.
3D structure databases
ProteinModelPortal	Q91VN0.
SMR	Q91VN0. Positions 31-1255.
ModBase	Search...
PTM databases
PhosphoSite	Q91VN0.
Proteomic databases
PaxDb	Q91VN0.
PRIDE	Q91VN0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025856; ENSMUSP00000025856; ENSMUSG00000024913.
GeneID	16973.
KEGG	mmu:16973.
Organism-specific databases
CTD	4041.
MGI	MGI:1278315. Lrp5.
Phylogenomic databases
eggNOG	NOG121718.
GeneTree	ENSGT00690000101695.
HOVERGEN	HBG049167.
InParanoid	Q91VN0.
KO	K03068.
OMA	LFWTCEA.
OrthoDB	EOG4RNB7H.
Gene expression databases
ArrayExpress	Q91VN0.
Bgee	Q91VN0.
Genevestigator	Q91VN0.
GermOnline	ENSMUSG00000024913. Mus musculus.
Family and domain databases
Gene3D	2.120.10.30. 4 hits. 4.10.400.10. 3 hits.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR000742. EG-like_dom. IPR023415. LDLR_class-A_CS. IPR000033. LDLR_classB_rpt. IPR002172. LDrepeatLR_classA_rpt. IPR017049. Low_density_Lipo_rcpt-rel_p5/6. [Graphical view]
Pfam	PF00057. Ldl_recept_a. 3 hits. PF00058. Ldl_recept_b. 14 hits. [Graphical view]
PIRSF	PIRSF036314. LDL_recpt-rel_p5/6. 1 hit.
SMART	SM00181. EGF. 4 hits. SM00192. LDLa. 3 hits. SM00135. LY. 20 hits. [Graphical view]
SUPFAM	SSF57424. LDL_rcpt_classA_cys-rich. 3 hits.
PROSITE	PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. False negative. PS01187. EGF_CA. False negative. PS01209. LDLRA_1. 3 hits. PS50068. LDLRA_2. 3 hits. PS51120. LDLRB. 20 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	291030.
SOURCE	Search...

Entry information

Entry name

LRP5_MOUSE

Accession

Primary (citable) accession number: Q91VN0
Secondary accession number(s): E9QQ75, O88883, Q9R208

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program