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P09571 (TRFE_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Serotransferrin
Short name=Transferrin
Alternative name(s):
Siderophilin
Beta-1 metal-binding globulin
Gene names
Name:TF
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length696 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandIron
Metal-binding
   PTMDisulfide bond
Glycoprotein
Methylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcellular iron ion homeostasis

Inferred from electronic annotation. Source: InterPro

iron ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionferric iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 696696Serotransferrin
PRO_0000082439

Regions

Domain6 – 332327Transferrin-like 1
Domain346 – 672327Transferrin-like 2

Sites

Metal binding621Iron 1 By similarity
Metal binding941Iron 1 By similarity
Metal binding1921Iron 1 By similarity
Metal binding2531Iron 1 By similarity
Metal binding3961Iron 2 By similarity
Metal binding4311Iron 2 By similarity
Metal binding5261Iron 2 By similarity
Metal binding5941Iron 2 By similarity
Binding site1191Carbonate 1 By similarity
Binding site1231Carbonate 1 By similarity
Binding site1251Carbonate 1; via amide nitrogen By similarity
Binding site1261Carbonate 1; via amide nitrogen By similarity
Binding site4581Carbonate 2 By similarity
Binding site4621Carbonate 2 By similarity
Binding site4641Carbonate 2; via amide nitrogen By similarity
Binding site4651Carbonate 2; via amide nitrogen By similarity

Amino acid modifications

Modified residue231Omega-N-methylated arginine By similarity
Modified residue5261Phosphotyrosine By similarity
Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Disulfide bond9 ↔ 47 By similarity
Disulfide bond19 ↔ 38 By similarity
Disulfide bond117 ↔ 198 By similarity
Disulfide bond157 ↔ 173 By similarity
Disulfide bond160 ↔ 181 By similarity
Disulfide bond170 ↔ 183 By similarity
Disulfide bond231 ↔ 245 By similarity
Disulfide bond343 ↔ 605 By similarity
Disulfide bond349 ↔ 381 By similarity
Disulfide bond359 ↔ 372 By similarity
Disulfide bond406 ↔ 682 By similarity
Disulfide bond423 ↔ 646 By similarity
Disulfide bond456 ↔ 532 By similarity
Disulfide bond480 ↔ 673 By similarity
Disulfide bond490 ↔ 504 By similarity
Disulfide bond501 ↔ 515 By similarity
Disulfide bond572 ↔ 586 By similarity
Disulfide bond624 ↔ 629 By similarity

Natural variations

Natural variant3081K → R

Experimental info

Sequence conflict201S → E AA sequence Ref.2

Secondary structure

1 .............................................................................................................................. 696
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09571-1 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 787C59F42D844B26

FASTA69676,968
        10         20         30         40         50         60 
VAQKTVRWCT ISNQEANKCS SFRENMSKAV KNGPLVSCVK KSSYLDCIKA IRDKEADAVT 

        70         80         90        100        110        120 
LDAGLVFEAG LAPYNLKPVV AEFYGQKDNP QTHYYAVAVV KKGSNFQWNQ LQGKRSCHTG 

       130        140        150        160        170        180 
LGRSAGWIIP MGLLYDQLPE PRKPIEKAVA SFFSSSCVPC ADPVNFPKLC QQCAGKGAEK 

       190        200        210        220        230        240 
CACSNHEPYF GYAGAFNCLK EDAGDVAFVK HSTVLENLPD KADRDQYELL CRDNTRRPVD 

       250        260        270        280        290        300 
DYENCYLAQV PSHAVVARSV DGQEDSIWEL LNQAQEHFGR DKSPDFQLFS SSHGKDLLFK 

       310        320        330        340        350        360 
DSANGFLKIP SKMDSSLYLG YQYVTALRNL REEISPDSSK NECKKVRWCA IGHEETQKCD 

       370        380        390        400        410        420 
AWSINSGGKI ECVSAENTED CIAKIVKGEA DAMSLDGGYI YIAGKCGLVP VLAENYKTEG 

       430        440        450        460        470        480 
ENCVNTPEKG YLAVAVVKKS SGPDLNWNNL KGKKSCHTAV DRTAGWNIPM GLLYNKINSC 

       490        500        510        520        530        540 
KFDQFFGEGC APGSQRNSSL CALCIGSERA PGRECLANNH ERYYGYTGAF RCLVEKGDVA 

       550        560        570        580        590        600 
FVKDQVVQQN TDGKNKDDWA KDLKQMDFEL LCQNGAREPV DNAENCHLAR APNHAVVARD 

       610        620        630        640        650        660 
DKVTCVAEEL LKQQAQFGRH VTDCSSSFCM FKSNTKDLLF RDDTQCLARV GKTTYESYLG 

       670        680        690 
ADYITAVANL RKCSTSKLLE ACTFHSAKNP RVETTT

« Hide

References

[1]"Nucleotide sequence of porcine liver transferrin."
Baldwin G.S., Weinstock J.
Nucleic Acids Res. 16:8720-8720(1988) [PubMed: 3419934] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Purification of transferrins and lactoferrin using DEAE affi-gel blue."
Chung M.C., Chan S.L., Shimizu S.
Int. J. Biochem. 23:609-616(1991) [PubMed: 2065820] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20.
[3]"Isolation of transferrin from porcine gastric mucosa: comparison with porcine serum transferrin."
Baldwin G.S., Bacic T., Chandler R., Grego B., Pedersen J., Simpson R.J., Toh B.H., Weinstock J.
Comp. Biochem. Physiol. 95B:261-268(1990) [PubMed: 2328566] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15.
[4]"The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively."
Hall D.R., Hadden J.M., Leonard G.A., Bailey S., Neu M., Winn M., Lindley P.F.
Acta Crystallogr. D 58:70-80(2002) [PubMed: 11752780] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X12386 mRNA. Translation: CAA30943.1.
PIRS01384.
UniGeneSsc.54403.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H76X-ray2.15A1-696[»]
ProteinModelPortalP09571.
ModBaseSearch...

Protein family/group databases

MEROPSS60.971.

Genome annotation databases

EnsemblENSSSCT00000012741; ENSSSCP00000012407; ENSSSCG00000011640; Sus scrofa. [Genome view]

Phylogenomic databases

HOVERGENHBG000055.

Family and domain databases

InterProIPR001156. Peptidase_S60.
IPR016357. Transferrin.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PANTHERPTHR11485. Peptidase_S60. 1 hit.
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRFE_PIG
AccessionPrimary (citable) accession number: P09571
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1991
Last modified: August 10, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents