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P35969 (VGFR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vascular endothelial growth factor receptor 1

Short name=VEGFR-1
EC=2.7.10.1
Alternative name(s):
Embryonic receptor kinase 2
Fms-like tyrosine kinase 1
Short name=FLT-1
Tyrosine-protein kinase receptor FLT
Gene names
Name:Flt1
Synonyms:Emrk2, Flt, Vegfr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, and proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts. Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to the activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC, YES1 and PLCG, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 and PTK2/FAK1 By similarity. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulation

Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFB or PGF leads to dimerization and activation by autophosphorylation on tyrosine residues By similarity.

Subunit structure

Interacts with VEGFA, VEGFB and PGF. Monomer in the absence of bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA, VEGFB and PGF. Can also form a heterodimer with KDR. Interacts (tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts with PTPRB. Interacts with GNB2L1/RACK1. Identified in a complex with CBL and CD2AP By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endosome By similarity. Note: Autophosphorylation promotes ubiquitination and endocytosis By similarity.

Domain

The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFA binding By similarity.

Post-translational modification

N-glycosylated By similarity.

Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation By similarity.

Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-1169 is important for interaction with PLCG. Phosphorylation at Tyr-1213 is important for interaction with PIK3R1, PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1328 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB By similarity.

Disruption phenotype

Embryonic lethality at about 9 dpc, due to defects in the formation and organization of the vascular network. Mice display abnormal blood island structures in the yolk sac, leading to defects in the organization of the vascular endothelium, excess growth and disorganization of embryonic and extraembryonic vasculature, including the endocardium and the microvasculature. Mice expressing a mutant protein that lacks the kinase domain survive and have no apparent phenotype. Ref.5 Ref.6 Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 7 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAngiogenesis
Chemotaxis
Differentiation
   Cellular componentCell membrane
Endosome
Membrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Traceable author statement Ref.6. Source: UniProtKB

blood vessel morphogenesis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype Ref.6. Source: UniProtKB

embryonic morphogenesis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

monocyte chemotaxis

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from mutant phenotype Ref.8. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of phospholipase C activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

sprouting angiogenesis

Inferred from mutant phenotype PubMed 19758562. Source: MGI

vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.6. Source: MGI

vascular endothelial growth factor signaling pathway

Inferred from direct assay PubMed 8356051. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

VEGF-A-activated receptor activity

Inferred from electronic annotation. Source: Ensembl

VEGF-B-activated receptor activity

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 11591653. Source: MGI

placental growth factor-activated receptor activity

Inferred from electronic annotation. Source: Ensembl

vascular endothelial growth factor-activated receptor activity

Inferred from direct assay PubMed 8356051. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 13331311Vascular endothelial growth factor receptor 1
PRO_0000016769

Regions

Topological domain23 – 759737Extracellular Potential
Transmembrane760 – 78122Helical; Potential
Topological domain782 – 1333552Cytoplasmic Potential
Domain32 – 12493Ig-like C2-type 1
Domain152 – 21564Ig-like C2-type 2
Domain231 – 32898Ig-like C2-type 3
Domain334 – 42996Ig-like C2-type 4
Domain430 – 550121Ig-like C2-type 5
Domain557 – 656100Ig-like C2-type 6
Domain662 – 74887Ig-like C2-type 7
Domain828 – 1158331Protein kinase
Nucleotide binding834 – 8429ATP By similarity

Sites

Active site10221Proton acceptor By similarity
Binding site8621ATP By similarity
Site768 – 7692Cleavage; by PSEN1 By similarity

Amino acid modifications

Modified residue9151Phosphotyrosine; by autocatalysis By similarity
Modified residue10531Phosphotyrosine; by autocatalysis By similarity
Modified residue11691Phosphotyrosine; by autocatalysis By similarity
Modified residue12131Phosphotyrosine; by autocatalysis By similarity
Modified residue12421Phosphotyrosine; by autocatalysis By similarity
Modified residue13221Phosphotyrosine; by autocatalysis By similarity
Modified residue13281Phosphotyrosine; by autocatalysis By similarity
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential
Glycosylation5171N-linked (GlcNAc...) Potential
Glycosylation5981N-linked (GlcNAc...) Potential
Glycosylation6261N-linked (GlcNAc...) Potential
Glycosylation6671N-linked (GlcNAc...) Potential
Glycosylation7141N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 108 By similarity
Disulfide bond159 ↔ 208 By similarity
Disulfide bond253 ↔ 312 By similarity
Disulfide bond455 ↔ 536 By similarity
Disulfide bond578 ↔ 637 By similarity
Disulfide bond683 ↔ 732 By similarity

Experimental info

Sequence conflict1581Missing in CAA55311. Ref.2
Sequence conflict2111Missing in CAA55311. Ref.2
Sequence conflict2451H → L in CAA55311. Ref.2
Sequence conflict6031H → N in CAA55311. Ref.2
Sequence conflict609 – 6157KMATTQD → NGHHSS in CAA55311. Ref.2
Sequence conflict6961F → L in CAA55311. Ref.2
Sequence conflict7341A → S in CAA55311. Ref.2
Sequence conflict7651C → Y in CAA55311. Ref.2
Sequence conflict8201K → N in CAA55311. Ref.2
Sequence conflict10091G → R in CAA55311. Ref.2
Sequence conflict11811S → G in BAA24498. Ref.3
Sequence conflict11811S → N in CAA55311. Ref.2
Sequence conflict1193 – 11942LF → RG in CAA55311. Ref.2
Sequence conflict1278 – 12792KS → PR in CAA55311. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35969 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: C06533B7ECBC404C

FASTA1,333149,876
        10         20         30         40         50         60 
MVSCWDTAVL PYALLGCLLL TGYGSGSKLK VPELSLKGTQ HVMQAGQTLF LKCRGEAAHS 

        70         80         90        100        110        120 
WSLPTTVSQE DKRLSITPPS ACGRDNRQFC STLTLDTAQA NHTGLYTCRY LPTSTSKKKK 

       130        140        150        160        170        180 
AESSIYIFVS DAGSPFIEMH TDIPKLVHMT EGRQLIIPCR VTSPNVTVTL KKFPFDTLTP 

       190        200        210        220        230        240 
DGQRITWDSR RGFIIANATY KEIGLLNCEA TVNGHLYQTN YLTHRQTNTI LDVQIRPPSP 

       250        260        270        280        290        300 
VRLLHGQTLV LNCTATTELN TRVQMSWNYP GKATKRASIR QRIDRSHSHN NVFHSVLKIN 

       310        320        330        340        350        360 
NVESRDKGLY TCRVKSGSSF QSFNTSVHVY EKGFISVKHR KQPVQETTAG RRSYRLSMKV 

       370        380        390        400        410        420 
KAFPSPEIVW LKDGSPATLK SARYLVHGYS LIIKDVTTED AGDYTILLGI KQSRLFKNLT 

       430        440        450        460        470        480 
ATLIVNVKPQ IYEKSVSSLP SPPLYPLGSR QVLTCTVYGI PRPTITWLWH PCHHNHSKER 

       490        500        510        520        530        540 
YDFCTENEES FILDPSSNLG NRIESISQRM TVIEGTNKTV STLVVADSQT PGIYSCRAFN 

       550        560        570        580        590        600 
KIGTVERNIK FYVTDVPNGF HVSLEKMPAE GEDLKLSCVV NKFLYRDITW ILLRTVNNRT 

       610        620        630        640        650        660 
MHHSISKQKM ATTQDYSITL NLVIKNVSLE DSGTYACRAR NIYTGEDILR KTEVLVRDSE 

       670        680        690        700        710        720 
APHLLQNLSD YEVSISGSTT LDCQARGVPA PQITWFKNNH KIQQEPGIIL GPGNSTLFIE 

       730        740        750        760        770        780 
RVTEEDEGVY RCRATNQKGA VESAAYLTVQ GTSDKSNLEL ITLTCTCVAA TLFWLLLTLF 

       790        800        810        820        830        840 
IRKLKRSSSE VKTDYLSIIM DPDEVPLDEQ CERLPYDASK WEFARERLKL GKSLGRGAFG 

       850        860        870        880        890        900 
KVVQASAFGI KKSPTCRTVA VKMLKEGATA SEYKALMTEL KILTHIGHHL NVVNLLGACT 

       910        920        930        940        950        960 
KQGGPLMVIV EYCKYGNLSN YLKSKRDLFC LNKDAALHME LKKESLEPGL EQGQKPRLDS 

       970        980        990       1000       1010       1020 
VSSSSVTSSS FPEDRSVSDV EGDEDYSEIS KQPLTMEDLI SYSFQVARGM EFLSSRKCIH 

      1030       1040       1050       1060       1070       1080 
RDLAARNILL SENNVVKICD FGLARDIYKN PDYVRRGDTR LPLKWMAPES IFDKVYSTKS 

      1090       1100       1110       1120       1130       1140 
DVWSYGVLLW EIFSLGGSPY PGVQMDEDFC SRLKEGMRMR TPEYATPEIY QIMLDCWHKD 

      1150       1160       1170       1180       1190       1200 
PKERPRFAEL VEKLGDLLQA NVQQDGKDYI PLNAILTRNS SFTYSTPTFS EDLFKDGFAD 

      1210       1220       1230       1240       1250       1260 
PHFHSGSSDD VRYVNAFKFM SLERIKTFEE LSPNSTSMFE DYQLDTSTLL GSPLLKRFTW 

      1270       1280       1290       1300       1310       1320 
TETKPKASMK IDLRIASKSK EAGLSDLPRP SFCFSSCGHI RPVQDDESEL GKESCCSPPP 

      1330 
DYNSVVLYSS PPA 

« Hide

References

[1]"Molecular cloning of murine FLT and FLT4."
Finnerty H., Kelleher K., Morris G.E., Bean K., Merberg D.M., Kriz R., Morris J.C., Sookdeo H., Turner K.J., Wood C.R.
Oncogene 8:2293-2298(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Neonatal brain and Placenta.
[2]"Isolation of a gene encoding a novel receptor tyrosine kinase from differentiated embryonic stem cells."
Choi K., Wall C., Hanratty R., Keller G.
Oncogene 9:1261-1266(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Genomic organization of the flt-1 gene encoding for vascular endothelial growth factor (VEGF) receptor-1 suggests an intimate evolutionary relationship between the 7-Ig and the 5-Ig tyrosine kinase receptors."
Kondo K., Hiratsuka S., Subbalakshmi E., Matsushime H., Shibuya M.
Gene 208:297-305(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Lung.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 110-119 AND 185-191, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium."
Fong G.H., Rossant J., Gertsenstein M., Breitman M.L.
Nature 376:66-70(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN BLOOD VESSEL DEVELOPMENT DURING EMBRYOGENESIS.
[6]"Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice."
Hiratsuka S., Minowa O., Kuno J., Noda T., Shibuya M.
Proc. Natl. Acad. Sci. U.S.A. 95:9349-9354(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN MACROPHAGE MIGRATION.
[7]"Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis."
Hiratsuka S., Maru Y., Okada A., Seiki M., Noda T., Shibuya M.
Cancer Res. 61:1207-1213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
[8]"The VEGF receptor flt-1 (VEGFR-1) is a positive modulator of vascular sprout formation and branching morphogenesis."
Kearney J.B., Kappas N.C., Ellerstrom C., DiPaola F.W., Bautch V.L.
Blood 103:4527-4535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[9]"Vascular endothelial growth factor receptor-1 regulates postnatal angiogenesis through inhibition of the excessive activation of Akt."
Nishi J., Minamino T., Miyauchi H., Nojima A., Tateno K., Okada S., Orimo M., Moriya J., Fong G.H., Sunagawa K., Shibuya M., Komuro I.
Circ. Res. 103:261-268(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
[10]"Vascular endothelial growth factor receptor-1 signaling promotes mobilization of macrophage lineage cells from bone marrow and stimulates solid tumor growth."
Muramatsu M., Yamamoto S., Osawa T., Shibuya M.
Cancer Res. 70:8211-8221(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07297 mRNA. Translation: AAA40078.1.
X78568 mRNA. Translation: CAA55311.1.
D88689 mRNA. Translation: BAA24498.1.
CCDSCCDS19879.1.
PIRI78875.
S49010.
RefSeqNP_034358.2. NM_010228.3.
UniGeneMm.389712.

3D structure databases

ProteinModelPortalP35969.
SMRP35969. Positions 32-751, 788-1197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199706. 5 interactions.
DIPDIP-39359N.
IntActP35969. 8 interactions.
MINTMINT-4139959.

Chemistry

BindingDBP35969.
ChEMBLCHEMBL3516.

PTM databases

PhosphoSiteP35969.

Proteomic databases

PaxDbP35969.
PRIDEP35969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031653; ENSMUSP00000031653; ENSMUSG00000029648.
GeneID14254.
KEGGmmu:14254.
UCSCuc009aoh.1. mouse.

Organism-specific databases

CTD2321.
MGIMGI:95558. Flt1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108679.
HOGENOMHOG000037949.
HOVERGENHBG053432.
InParanoidP35969.
KOK05096.
OrthoDBEOG75F4CC.
PhylomeDBP35969.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressP35969.
BgeeP35969.
CleanExMM_FLT1.
GenevestigatorP35969.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009135. VEGFR1_rcpt.
[Graphical view]
PANTHERPTHR24416:SF126. PTHR24416:SF126. 1 hit.
PfamPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSPR01833. VEGFRECEPTR1.
SMARTSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFLT1. mouse.
NextBio285579.
PROP35969.
SOURCESearch...

Entry information

Entry nameVGFR1_MOUSE
AccessionPrimary (citable) accession number: P35969
Secondary accession number(s): O55094, Q61517
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot