Q07014 (LYN_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Lyn
EC=2.7.10.2

Alternative name(s):
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn

Gene names

Name:

Lyn

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B By similarity. Phosphorylates LPXN on 'Tyr-72' By similarity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.4
Enzyme regulation	Subject to autoinhibition, mediated by intramolecular interactions between the SH2 domain and the C-terminal phosphotyrosine. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylated by CSK at Tyr-508; phosphorylation at Tyr-508 inhibits kinase activity. Kinase activity is modulated by dephosphorylation by PTPRC/CD45. Ref.4
Subunit structure	Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region) By similarity. Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation By similarity. Interacts (via ankyrin repeat region) with LYN (via SH3-domain) in an activation-independent status of LYN By similarity. Forms a multiprotein complex with LYN and HS1 By similarity.
Subcellular location	Cell membrane By similarity. Nucleus By similarity. Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Golgi apparatus By similarity. Note: Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport By similarity.
Tissue specificity	Detected in spleen (at protein level). Expressed predominantly in B-lymphoid and myeloid cells. Ref.4
Domain	The protein kinase domain plays an important role in its localization in the cell membrane By similarity.
Post-translational modification	Ubiquitinated. Ubiquitination is SH3-dependent By similarity. Phosphorylated on tyrosine residues in response to KIT signaling By similarity. Autophosphorylated. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A By similarity. Ref.4
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity Inflammatory response Innate immunity
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell homeostasis Inferred from sequence or structural similarity. Source: UniProtKB B cell receptor signaling pathway Inferred from electronic annotation. Source: Compara Fc receptor mediated inhibitory signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB Fc receptor mediated stimulatory signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB cellular response to extracellular stimulus Inferred from expression pattern PubMed 17845203. Source: RGD cellular response to heat Inferred from expression pattern PubMed 12372808. Source: RGD cellular response to retinoic acid Inferred from electronic annotation. Source: Compara cytokine secretion Inferred from mutant phenotype PubMed 16177098. Source: RGD dendritic cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB histamine secretion by mast cell Inferred from mutant phenotype PubMed 16177098. Source: RGD innate immune response Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Inferred from electronic annotation. Source: Compara lipopolysaccharide-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of B cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of mast cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of myeloid leukocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of toll-like receptor 2 signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of toll-like receptor 4 signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB neuron projection development Inferred from electronic annotation. Source: Compara oligodendrocyte development Inferred from expression pattern PubMed 15504915. Source: RGD peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara platelet degranulation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of Fc receptor mediated stimulatory signaling pathway Inferred from mutant phenotype PubMed 16177098. Source: RGD positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of dendritic cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of glial cell proliferation Inferred from direct assay PubMed 15504915. Source: RGD positive regulation of mast cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of oligodendrocyte progenitor proliferation Inferred from mutant phenotype PubMed 15504915. Source: RGD positive regulation of phosphatidylinositol 3-kinase activity Inferred from electronic annotation. Source: Compara positive regulation of stress-activated protein kinase signaling cascade Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of STAT protein Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from electronic annotation. Source: Compara regulation of B cell apoptotic process Inferred from electronic annotation. Source: Compara regulation of B cell receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell adhesion mediated by integrin Inferred from electronic annotation. Source: Compara regulation of cytokine production Inferred from sequence or structural similarity. Source: UniProtKB regulation of cytokine secretion Inferred from electronic annotation. Source: Compara regulation of erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of inflammatory response Inferred from electronic annotation. Source: Compara regulation of mast cell degranulation Inferred from sequence or structural similarity. Source: UniProtKB regulation of monocyte chemotaxis Inferred from electronic annotation. Source: Compara regulation of platelet aggregation Inferred from sequence or structural similarity. Source: UniProtKB regulation of release of sequestered calcium ion into cytosol Inferred from mutant phenotype PubMed 16177098. Source: RGD response to DNA damage stimulus Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from expression pattern PubMed 16529858. Source: RGD response to axon injury Inferred from expression pattern PubMed 17918263. Source: RGD response to carbohydrate stimulus Inferred from expression pattern PubMed 10330413. Source: RGD response to insulin stimulus Inferred from expression pattern PubMed 12089355. Source: RGD response to organic cyclic compound Inferred from expression pattern PubMed 15287886PubMed 17265464. Source: RGD response to sterol depletion Inferred from expression pattern PubMed 10330413. Source: RGD response to toxin Inferred from expression pattern PubMed 16529858. Source: RGD tolerance induction to self antigen Inferred from sequence or structural similarity. Source: UniProtKB transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell alpha2-beta1 integrin complex Inferred from direct assay PubMed 18234883. Source: RGD membrane raft Inferred from direct assay PubMed 18326662. Source: RGD mitochondrial crista Inferred from direct assay PubMed 12007793. Source: RGD mitochondrial intermembrane space Inferred from direct assay PubMed 12007793. Source: RGD nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from direct assay PubMed 14529711. Source: RGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glycosphingolipid binding Inferred from physical interaction PubMed 8106508. Source: RGD integrin binding Inferred from direct assay PubMed 15504915. Source: RGD non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay PubMed 12007793. Source: RGD
Complete GO annotation...

Alternative products

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

Isoform LYN A (identifier: Q07014-1)

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 LYN B (identifier: Q07014-2)

The sequence of this isoform differs from the canonical sequence as follows:
     25-45: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 512	512	Tyrosine-protein kinase Lyn		PRO_0000088131
Regions
	Domain	63 – 123	61	SH3
	Domain	129 – 226	98	SH2
	Domain	247 – 501	255	Protein kinase
	Nucleotide binding	253 – 261	9	ATP By similarity
Sites
	Active site	367	1	Proton acceptor By similarity
	Binding site	275	1	ATP By similarity
Amino acid modifications
	Modified residue	6	1	Phosphoserine By similarity
	Modified residue	30	1	Phosphothreonine By similarity
	Modified residue	32	1	Phosphotyrosine By similarity
	Modified residue	37	1	Phosphothreonine By similarity
	Modified residue	193	1	Phosphotyrosine By similarity
	Modified residue	194	1	Phosphotyrosine By similarity
	Modified residue	228	1	Phosphoserine By similarity
	Modified residue	265	1	Phosphotyrosine By similarity
	Modified residue	306	1	Phosphotyrosine By similarity
	Modified residue	316	1	Phosphotyrosine By similarity
	Modified residue	397	1	Phosphotyrosine; by autocatalysis Ref.4
	Modified residue	460	1	Phosphotyrosine By similarity
	Modified residue	473	1	Phosphotyrosine By similarity
	Modified residue	489	1	Phosphothreonine By similarity
	Modified residue	502	1	Phosphothreonine By similarity
	Modified residue	508	1	Phosphotyrosine; by autocatalysis, CSK and MATK Ref.4
	Lipidation	2	1	N-myristoyl glycine By similarity
	Lipidation	3	1	S-palmitoyl cysteine By similarity
Natural variations
	Alternative sequence	25 – 45	21	Missing in isoform LYN B.		VSP_005004
Experimental info
	Sequence conflict	231	1	P → L in AAA20944. Ref.2
	Sequence conflict	231	1	P → L in AAA20945. Ref.2
	Sequence conflict	308	1	V → A in AAA20944. Ref.2
	Sequence conflict	308	1	V → A in AAA20945. Ref.2
	Sequence conflict	419	1	C → Y in AAA20944. Ref.2
	Sequence conflict	419	1	C → Y in AAA20945. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform LYN A [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E03615E229CD43F1	FASTA	512	58,660
	10 20 30 40 50 60 MGCIKSKRKD NLNDDGVDMK TQPVRNTDRT IYVRDPTSNK QQRPVPESQL LPGQRFQAKD 70 80 90 100 110 120 PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLSSKRE GFIPSNYVAK 130 140 150 160 170 180 VNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DYDPMHGDVI 190 200 210 220 230 240 KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW 250 260 270 280 290 300 EIPRESIKLV KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSAQAFLEE ANLMKTLQHD 310 320 330 340 350 360 KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGSKVL LPKLIDFSAQ IAEGMAYIER 370 380 390 400 410 420 KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF 430 440 450 460 470 480 TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMTALSQGY RMPRMENCPD ELYDIMKMCW 490 500 510 KESAEERPTF DYLQSVLDDF YTATEGQYQQ QP
	Isoform LYN B [UniParc]. Checksum: 6FFFB1609E015180	FASTA	491	56,133
	10 20 30 40 50 60 MGCIKSKRKD NLNDDGVDMK TQPVPESQLL PGQRFQAKDP EEQGDIVVAL YPYDGIHPDD 70 80 90 100 110 120 LSFKKGEKMK VLEEHGEWWK AKSLSSKREG FIPSNYVAKV NTLETEEWFF KDITRKDAER 130 140 150 160 170 180 QLLAPGNSAG AFLIRESETL KGSFSLSVRD YDPMHGDVIK HYKIRSLDNG GYYISPRITF 190 200 210 220 230 240 PCISDMIKHY QKQSDGLCRR LEKACISPKP QKPWDKDAWE IPRESIKLVK KLGAGQFGEV 250 260 270 280 290 300 WMGYYNNSTK VAVKTLKPGT MSAQAFLEEA NLMKTLQHDK LVRLYAVVTK EEPIYIITEF 310 320 330 340 350 360 MAKGSLLDFL KSDEGSKVLL PKLIDFSAQI AEGMAYIERK NYIHRDLRAA NVLVSESLMC 370 380 390 400 410 420 KIADFGLARV IEDNEYTARE GAKFPIKWTA PEAINFGCFT IKSDVWSFGI LLYEIVTYGK 430 440 450 460 470 480 IPYPGRTNAD VMTALSQGYR MPRMENCPDE LYDIMKMCWK ESAEERPTFD YLQSVLDDFY 490 TATEGQYQQQ P

References

[1]	"Bacterially expressed rat p56lyn binds several proteins in rat basophilic leukemia cells including pp72, a tyrosine phosphorylated protein prominent in activated cells." Minoguchi K., Nishikata H., Siraganian R.P. J. Immunol. 150:222-222(1993) Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The cDNAs encoding two forms of the LYN protein tyrosine kinase are expressed in rat mast cells and human myeloid cells." Rider L.G., Raben N., Miller L., Jelsema C. Gene 138:219-222(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE." Vonakis B.M., Chen H., Haleem-Smith H., Metzger H. J. Biol. Chem. 272:24072-24080(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Spontaneous autophosphorylation of Lyn tyrosine kinase at both its activation segment and C-terminal tail confers altered substrate specificity." Donella-Deana A., Cesaro L., Ruzzene M., Brunati A.M., Marin O., Pinna L.A. Biochemistry 37:1438-1446(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L14951 mRNA. Translation: AAA41549.1. L14782 mRNA. Translation: AAA20944.1. L14823 mRNA. Translation: AAA20945.1. AF000300 mRNA. Translation: AAB71344.1. AF000301 mRNA. Translation: AAB71345.1. AF000302 mRNA. Translation: AAB71346.1.
IPI	IPI00195871. IPI00327644.
PIR	I56160. PT0198.
RefSeq	NP_001104568.1. NM_001111098.1. NP_110484.1. NM_030857.2.
UniGene	Rn.4338.
3D structure databases
ProteinModelPortal	Q07014.
SMR	Q07014. Positions 67-512.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000011130.
PTM databases
PhosphoSite	Q07014.
Proteomic databases
PaxDb	Q07014.
PRIDE	Q07014.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000011130; ENSRNOP00000011130; ENSRNOG00000008180.
GeneID	81515.
KEGG	rno:81515.
UCSC	RGD:621017. rat.
Organism-specific databases
CTD	4067.
RGD	621017. Lyn.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00620000087866.
HOGENOM	HOG000233858.
HOVERGEN	HBG008761.
InParanoid	Q07014.
KO	K05854.
OrthoDB	EOG4N04DP.
Enzyme and pathway databases
BRENDA	2.7.10.2. 5301.
Reactome	REACT_109781. Immune System.
Gene expression databases
Genevestigator	Q07014.
GermOnline	ENSRNOG00000008180. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR000980. SH2. IPR001452. SH3_domain. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q07014.
ChEMBL	CHEMBL4363.
NextBio	615007.

Entry information

Entry name

LYN_RAT

Accession

Primary (citable) accession number: Q07014
Secondary accession number(s): Q63320

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program