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Q921I1 (TRFE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Serotransferrin

Short name=Transferrin
Alternative name(s):
Beta-1 metal-binding globulin
Siderophilin
Gene names
Name:Tf
Synonyms:Trf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length697 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.9

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transport
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandIron
Metal-binding
   PTMDisulfide bond
Glycoprotein
Methylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from direct assay PubMed 19252502. Source: DFLAT

SMAD protein signal transduction

Inferred from direct assay PubMed 9420335. Source: MGI

actin filament organization

Inferred from direct assay PubMed 19252502. Source: DFLAT

activation of JUN kinase activity

Inferred from direct assay PubMed 19252502. Source: DFLAT

cellular iron ion homeostasis

Inferred from electronic annotation. Source: InterPro

iron ion transport

Inferred from mutant phenotype PubMed 11230685. Source: MGI

osteoclast differentiation

Inferred from direct assay PubMed 19252502. Source: DFLAT

positive regulation of bone resorption

Inferred from direct assay PubMed 19252502. Source: DFLAT

positive regulation of cell motility

Inferred from direct assay PubMed 19252502. Source: DFLAT

positive regulation of phosphorylation

Inferred from direct assay PubMed 19252502. Source: DFLAT

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 19252502. Source: DFLAT

   Cellular_componentcoated pit

Inferred from direct assay PubMed 20427320. Source: MGI

dense body

Inferred from sequence orthology PubMed 21266579. Source: MGI

early endosome

Inferred from direct assay PubMed 23416069. Source: MGI

endocytic vesicle

Inferred from direct assay PubMed 12121420. Source: MGI

endosome

Inferred from direct assay PubMed 15247266PubMed 16227996PubMed 18477453PubMed 23303939PubMed 23416069. Source: MGI

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from direct assay PubMed 11739192PubMed 19061864. Source: MGI

vesicle coat

Inferred from sequence orthology PubMed 22792322. Source: MGI

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 697678Serotransferrin
PRO_0000035716

Regions

Domain25 – 347323Transferrin-like 1
Domain360 – 682323Transferrin-like 2

Sites

Metal binding821Iron 1 By similarity
Metal binding1141Iron 1 By similarity
Metal binding2071Iron 1 By similarity
Metal binding2681Iron 1 By similarity
Metal binding4101Iron 2 By similarity
Metal binding4481Iron 2 By similarity
Metal binding5371Iron 2 By similarity
Metal binding6051Iron 2 By similarity
Binding site1391Carbonate 1 By similarity
Binding site1431Carbonate 1 By similarity
Binding site1451Carbonate 1; via amide nitrogen By similarity
Binding site1461Carbonate 1; via amide nitrogen By similarity
Binding site4741Carbonate 2 By similarity
Binding site4781Carbonate 2 By similarity
Binding site4801Carbonate 2; via amide nitrogen By similarity
Binding site4811Carbonate 2; via amide nitrogen By similarity

Amino acid modifications

Modified residue421Omega-N-methylated arginine By similarity
Glycosylation5131N-linked (GlcNAc...) Ref.10
Disulfide bond28 ↔ 67 By similarity
Disulfide bond38 ↔ 58 By similarity
Disulfide bond137 ↔ 213 By similarity
Disulfide bond156 ↔ 350 By similarity
Disulfide bond177 ↔ 193 By similarity
Disulfide bond180 ↔ 196 By similarity
Disulfide bond190 ↔ 198 By similarity
Disulfide bond246 ↔ 260 By similarity
Disulfide bond363 ↔ 395 By similarity
Disulfide bond373 ↔ 386 By similarity
Disulfide bond420 ↔ 692 By similarity
Disulfide bond435 ↔ 655 By similarity
Disulfide bond472 ↔ 543 By similarity
Disulfide bond496 ↔ 683 By similarity
Disulfide bond506 ↔ 520 By similarity
Disulfide bond517 ↔ 526 By similarity
Disulfide bond583 ↔ 597 By similarity
Disulfide bond633 ↔ 638 By similarity

Experimental info

Sequence conflict3 – 42LT → FA in AAL34533. Ref.1
Sequence conflict691K → R in AAA40488. Ref.5
Sequence conflict71 – 744ISAS → HASG in AAH08559. Ref.3
Sequence conflict721S → A in AAA40488. Ref.5
Sequence conflict851W → L in AAA40488. Ref.5
Sequence conflict1041Y → C in AAA40488. Ref.5
Sequence conflict1131Y → S in AAA40488. Ref.5
Sequence conflict123 – 1242GT → ER in AAA40488. Ref.5
Sequence conflict1351K → E in BAE29847. Ref.2
Sequence conflict2831W → L in AAB28966. Ref.6
Sequence conflict3071P → L in AAB28966. Ref.6
Sequence conflict350 – 3512CP → SA in AAA39438. Ref.7
Sequence conflict4871G → C in AAA40490. Ref.5
Sequence conflict5271A → D in AAA40491. Ref.5
Sequence conflict5291N → S in BAE29847. Ref.2
Sequence conflict5751K → N in AAA40491. Ref.5
Sequence conflict6971H → S in AAL34533. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q921I1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0996A0C3B64CB1B9

FASTA69776,724
        10         20         30         40         50         60 
MRLTVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP PDGPRLACVK 

        70         80         90        100        110        120 
KTSYPDCIKA ISASEADAMT LDGGWVYDAG LTPNNLKPVA AEFYGSVEHP QTYYYAVAVV 

       130        140        150        160        170        180 
KKGTDFQLNQ LEGKKSCHTG LGRSAGWVIP IGLLFCKLSE PRSPLEKAVS SFFSGSCVPC 

       190        200        210        220        230        240 
ADPVAFPKLC QLCPGCGCSS TQPFFGYVGA FKCLKDGGGD VAFVKHTTIF EVLPEKADRD 

       250        260        270        280        290        300 
QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARKNNGKED LIWEILKVAQ EHFGKGKSKD 

       310        320        330        340        350        360 
FQLFSSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHNYVT AIRNQQEGVC PEGSIDNSPV 

       370        380        390        400        410        420 
KWCALSHLER TKCDEWSIIS EGKIECESAE TTEDCIEKIV NGEADAMTLD GGHAYIAGQC 

       430        440        450        460        470        480 
GLVPVMAEYY ESSNCAIPSQ QGIFPKGYYA VAVVKASDTS ITWNNLKGKK SCHTGVDRTA 

       490        500        510        520        530        540 
GWNIPMGMLY NRINHCKFDE FFSQGCAPGY EKNSTLCDLC IGPLKCAPNN KEEYNGYTGA 

       550        560        570        580        590        600 
FRCLVEKGDV AFVKHQTVLD NTEGKNPAEW AKNLKQEDFE LLCPDGTRKP VKDFASCHLA 

       610        620        630        640        650        660 
QAPNHVVVSR KEKAARVKAV LTSQETLFGG SDCTGNFCLF KSTTKDLLFR DDTKCFVKLP 

       670        680        690 
EGTTPEKYLG AEYMQSVGNM RKCSTSRLLE ACTFHKH 

« Hide

References

« Hide 'large scale' references
[1]"Construction of a robust CHO cell-line for biopharmaceutical production."
Lai D.-Z.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion, Bone marrow, Liver and Mammary gland.
[3]"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].
Strain: FVB/N.
Tissue: Liver and Mammary tumor.
[4]"Comparative sequence analysis of the mouse and human transferrin promoters: hormonal regulation of the transferrin promoter in Sertoli cells."
Chaudhary J., Skinner M.K.
Mol. Reprod. Dev. 50:273-283(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
Strain: BALB/c.
[5]"Transferrin mRNA level in the mouse mammary gland is regulated by pregnancy and extracellular matrix."
Chen L.-H., Bissell M.J.
J. Biol. Chem. 262:17247-17250(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-131; 277-337; 462-496 AND 526-575.
[6]"Transferrin gene expression in maternal liver, fetal liver and placenta during pregnancy in the mouse."
Kasik J.W., Rice E.J.
Placenta 14:365-371(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 268-307.
Tissue: Placenta.
[7]"Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions."
Pentecost B.T., Teng C.T.
J. Biol. Chem. 262:10134-10139(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 282-412.
[8]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 332-343 AND 659-667, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[9]"Expression from the transferrin gene promoter in transgenic mice."
Idzerda R.L., Behringer R.R., Theisen M., Huggenvik J.I., McKnight G.S., Brinster R.L.
Mol. Cell. Biol. 9:5154-5162(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-513.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF440692 mRNA. Translation: AAL34533.1.
AK085754 mRNA. Translation: BAC39532.1.
AK142599 mRNA. Translation: BAE25124.1.
AK146549 mRNA. Translation: BAE27253.1.
AK149559 mRNA. Translation: BAE28960.1.
AK149595 mRNA. Translation: BAE28981.1.
AK150782 mRNA. Translation: BAE29847.1.
AK168419 mRNA. Translation: BAE40332.1.
AK168938 mRNA. Translation: BAE40747.1.
BC008559 mRNA. Translation: AAH08559.1.
BC012313 mRNA. Translation: AAH12313.1.
BC022986 mRNA. Translation: AAH22986.1.
BC092046 mRNA. Translation: AAH92046.1.
AF027336 Genomic DNA. Translation: AAB84034.1.
M23013 mRNA. Translation: AAA40488.1.
M23014 mRNA. Translation: AAA40489.1.
M23015 mRNA. Translation: AAA40490.1.
M23016 mRNA. Translation: AAA40491.1.
S67217 mRNA. Translation: AAB28966.2.
J03299 mRNA. Translation: AAA39438.1.
PIRA28446.
RefSeqNP_598738.1. NM_133977.2.
UniGeneMm.37214.

3D structure databases

ProteinModelPortalQ921I1.
SMRQ921I1. Positions 20-694.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ921I1. 8 interactions.
MINTMINT-1202663.

Protein family/group databases

MEROPSS60.972.

PTM databases

PhosphoSiteQ921I1.

2D gel databases

REPRODUCTION-2DPAGEIPI00139788.
Q921I1.

Proteomic databases

PaxDbQ921I1.
PRIDEQ921I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035158; ENSMUSP00000035158; ENSMUSG00000032554.
ENSMUST00000112645; ENSMUSP00000108264; ENSMUSG00000032554.
GeneID22041.
KEGGmmu:22041.
UCSCuc009rgi.1. mouse.

Organism-specific databases

CTD22041.
MGIMGI:98821. Trf.

Phylogenomic databases

eggNOGNOG87503.
GeneTreeENSGT00390000001619.
HOVERGENHBG000055.
InParanoidQ921I1.
KOK14736.
OrthoDBEOG7D59N7.
PhylomeDBQ921I1.
TreeFamTF324013.

Gene expression databases

BgeeQ921I1.
CleanExMM_TRF.
GenevestigatorQ921I1.

Family and domain databases

InterProIPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio301824.
PROQ921I1.
SOURCESearch...

Entry information

Entry nameTRFE_MOUSE
AccessionPrimary (citable) accession number: Q921I1
Secondary accession number(s): O35421 expand/collapse secondary AC list , Q3UBW7, Q58E69, Q61803, Q62357, Q62358, Q62359, Q63915, Q64515, Q8VII5, Q922C0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 124 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

MGD cross-references

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