Reviewed, UniProtKB/Swiss-Prot A1Y2K1 (FYN_PIG)

Names and origin

Protein names

Recommended name:
    Proto-oncogene tyrosine-protein kinase Fyn
    EC=2.7.10.2
Alternative name(s):
    p59-Fyn

Gene names

Name:

FYN

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Blocks axon outgrowth and attraction induced by NTN1 by phosphorylating its receptor DDC By similarity. UniProtKB P06241 UniProtKB P39688 UniProtKB Q62844
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. UniProtKB P06241
Cofactor	Manganese By similarity. UniProtKB P06241
Enzyme regulation	Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site By similarity.
Subunit structure	Associates through its SH3 domain, to the p85 subunit of phosphatidylinositol 3-kinase. Interacts with the FYN-binding protein (FYB). Interacts with phosphorylated TOM1L1. Interacts with PAG1. Interacts with CD79A upon activation of the B-cell antigen receptor which increases FYN activity By similarity. Interacts with SH2D1A and SLAMF1. Interacts (via SH3 domain) with PRMT8 By similarity.
Subcellular location	Cell membrane By similarity. Note: Present and active in lipid rafts. Present in cell body and along the process of mature and developing oligodendroyctes By similarity.
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
Cellular component	Cell membrane Membrane
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Gene Ontology (GO)
Biological process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity UniProtKB P06241
	Chain	2 – 537	536	Proto-oncogene tyrosine-protein kinase Fyn UniProtKB P06241		PRO_0000282943
Regions
	Domain	82 – 143	62	SH3
	Domain	149 – 246	98	SH2
	Domain	271 – 524	254	Protein kinase
	Nucleotide binding	277 – 285	9	ATP By similarity UniProtKB P28523
Sites
	Active site	390	1	Proton acceptor By similarity UniProtKB P28523
	Binding site	299	1	ATP By similarity UniProtKB Q62844
Amino acid modifications
	Modified residue	12	1	Phosphothreonine; by PKC By similarity UniProtKB P06241
	Modified residue	21	1	Phosphoserine By similarity UniProtKB P06241
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	185	1	Phosphotyrosine By similarity
	Modified residue	213	1	Phosphotyrosine By similarity
	Modified residue	214	1	Phosphotyrosine By similarity
	Modified residue	254	1	Phosphothreonine By similarity
	Modified residue	257	1	Phosphoserine By similarity
	Modified residue	420	1	Phosphotyrosine; by autocatalysis By similarity UniProtKB P06241
	Modified residue	440	1	Phosphotyrosine By similarity
	Modified residue	531	1	Phosphotyrosine By similarity UniProtKB P39688
	Lipidation	2	1	N-myristoyl glycine By similarity UniProtKB P39688
	Lipidation	3	1	S-palmitoyl cysteine By similarity UniProtKB P39688
	Lipidation	6	1	S-palmitoyl cysteine By similarity UniProtKB P39688

Sequences

	Sequence		Length	Mass (Da)
	A1Y2K1-1 [UniParc]. Last modified February 20, 2007. Version 2. Checksum: 1CD6E4665939438F	FASTA	537	60,689
	10 20 30 40 50 60 MGCVQCKDKE ATKLTEERDG SLNQSSGFRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG 70 80 90 100 110 120 LTVFGGVSSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 130 140 150 160 170 180 EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 190 200 210 220 230 240 TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC 250 260 270 280 290 300 RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 310 320 330 340 350 360 LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR 370 380 390 400 410 420 ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY 430 440 450 460 470 480 TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE 490 500 510 520 530 RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL

References

[1]	"Cloning and expression of porcine FYN gene." Long H., Yang Z. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ836055 mRNA. Translation: ABI33874.2.
RefSeq	NP_001073675.2.
UniGene	Ssc.44857
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	791125.
KEGG	ssc:791125.
Organism-specific databases
CTD	791125.
Phylogenomic databases
HOVERGEN	A1Y2K1.
Enzyme and pathway databases
BRENDA	2.7.10.2. 249.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR000980. SH2. IPR001452. SH3_domain. IPR020473. SH3_region. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. [Graphical view]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. PD000093. SH2. 1 hit. PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
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...

Entry information

Entry name

FYN_PIG

Accession

Primary (citable) accession number: A1Y2K1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	February 20, 2007
Last modified:	October 13, 2009
This is version 26 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)