Q921I1 (TRFE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serotransferrin
Short name=Transferrin

Alternative name(s):
Beta-1 metal-binding globulin
Siderophilin

Gene names

Name:	Tf
Synonyms:	Trf

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	697 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Ion transport Iron transport Transport
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Iron Metal-binding
PTM	Disulfide bond Glycoprotein Methylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ERK1 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 transcription, DNA-dependent Inferred from direct assay PubMed 19252502. Source: DFLAT
Cellular_component	coated pit Inferred from direct assay PubMed 20427320. Source: MGI endocytic vesicle Inferred from direct assay PubMed 12121420. Source: MGI endoplasmic reticulum part Inferred from sequence orthology PubMed 22792322. Source: MGI extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome Inferred from direct assay PubMed 11739192PubMed 19061864. Source: MGI
Molecular_function	ferric iron 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
	Signal peptide	1 – 19	19	By similarity
	Chain	20 – 697	678	Serotransferrin		PRO_0000035716
Regions
	Domain	25 – 347	323	Transferrin-like 1
	Domain	360 – 682	323	Transferrin-like 2
Sites
	Metal binding	82	1	Iron 1 By similarity
	Metal binding	114	1	Iron 1 By similarity
	Metal binding	207	1	Iron 1 By similarity
	Metal binding	268	1	Iron 1 By similarity
	Metal binding	410	1	Iron 2 By similarity
	Metal binding	448	1	Iron 2 By similarity
	Metal binding	537	1	Iron 2 By similarity
	Metal binding	605	1	Iron 2 By similarity
	Binding site	139	1	Carbonate 1 By similarity
	Binding site	143	1	Carbonate 1 By similarity
	Binding site	145	1	Carbonate 1; via amide nitrogen By similarity
	Binding site	146	1	Carbonate 1; via amide nitrogen By similarity
	Binding site	474	1	Carbonate 2 By similarity
	Binding site	478	1	Carbonate 2 By similarity
	Binding site	480	1	Carbonate 2; via amide nitrogen By similarity
	Binding site	481	1	Carbonate 2; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	42	1	Omega-N-methylated arginine By similarity
	Glycosylation	513	1	N-linked (GlcNAc...) Ref.10
	Disulfide bond	28 ↔ 67		By similarity
	Disulfide bond	38 ↔ 58		By similarity
	Disulfide bond	137 ↔ 213		By similarity
	Disulfide bond	156 ↔ 350		By similarity
	Disulfide bond	177 ↔ 193		By similarity
	Disulfide bond	180 ↔ 196		By similarity
	Disulfide bond	190 ↔ 198		By similarity
	Disulfide bond	246 ↔ 260		By similarity
	Disulfide bond	363 ↔ 395		By similarity
	Disulfide bond	373 ↔ 386		By similarity
	Disulfide bond	420 ↔ 692		By similarity
	Disulfide bond	435 ↔ 655		By similarity
	Disulfide bond	472 ↔ 543		By similarity
	Disulfide bond	496 ↔ 683		By similarity
	Disulfide bond	506 ↔ 520		By similarity
	Disulfide bond	517 ↔ 526		By similarity
	Disulfide bond	583 ↔ 597		By similarity
	Disulfide bond	633 ↔ 638		By similarity
Experimental info
	Sequence conflict	3 – 4	2	LT → FA in AAL34533. Ref.1
	Sequence conflict	69	1	K → R in AAA40488. Ref.5
	Sequence conflict	71 – 74	4	ISAS → HASG in AAH08559. Ref.3
	Sequence conflict	72	1	S → A in AAA40488. Ref.5
	Sequence conflict	85	1	W → L in AAA40488. Ref.5
	Sequence conflict	104	1	Y → C in AAA40488. Ref.5
	Sequence conflict	113	1	Y → S in AAA40488. Ref.5
	Sequence conflict	123 – 124	2	GT → ER in AAA40488. Ref.5
	Sequence conflict	135	1	K → E in BAE29847. Ref.2
	Sequence conflict	283	1	W → L in AAB28966. Ref.6
	Sequence conflict	307	1	P → L in AAB28966. Ref.6
	Sequence conflict	350 – 351	2	CP → SA in AAA39438. Ref.7
	Sequence conflict	487	1	G → C in AAA40490. Ref.5
	Sequence conflict	527	1	A → D in AAA40491. Ref.5
	Sequence conflict	529	1	N → S in BAE29847. Ref.2
	Sequence conflict	575	1	K → N in AAA40491. Ref.5
	Sequence conflict	697	1	H → S in AAL34533. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q921I1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0996A0C3B64CB1B9	FASTA	697	76,724
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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.
IPI	IPI00139788.
PIR	A28446.
RefSeq	NP_598738.1. NM_133977.2.
UniGene	Mm.37214.
3D structure databases
ProteinModelPortal	Q921I1.
SMR	Q921I1. Positions 20-694.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q921I1. 3 interactions.
MINT	MINT-1202663.
Protein family/group databases
MEROPS	S60.972.
PTM databases
PhosphoSite	Q921I1.
2D gel databases
REPRODUCTION-2DPAGE	IPI00139788. Q921I1.
Proteomic databases
PaxDb	Q921I1.
PRIDE	Q921I1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035158; ENSMUSP00000035158; ENSMUSG00000032554. ENSMUST00000112645; ENSMUSP00000108264; ENSMUSG00000032554.
GeneID	22041.
KEGG	mmu:22041.
UCSC	uc009rgi.1. mouse.
Organism-specific databases
CTD	22041.
MGI	MGI:98821. Trf.
Phylogenomic databases
eggNOG	NOG87503.
GeneTree	ENSGT00390000001619.
HOVERGEN	HBG000055.
InParanoid	Q921I1.
KO	K14736.
OrthoDB	EOG4CRKZG.
Gene expression databases
ArrayExpress	Q921I1.
Bgee	Q921I1.
CleanEx	MM_TRF.
Genevestigator	Q921I1.
GermOnline	ENSMUSG00000032554. Mus musculus.
Family and domain databases
InterPro	IPR016357. Transferrin. IPR001156. Transferrin_fam. IPR018195. Transferrin_Fe_BS. [Graphical view]
PANTHER	PTHR11485. PTHR11485. 1 hit.
Pfam	PF00405. Transferrin. 2 hits. [Graphical view]
PIRSF	PIRSF002549. Transferrin. 1 hit.
PRINTS	PR00422. TRANSFERRIN.
SMART	SM00094. TR_FER. 2 hits. [Graphical view]
PROSITE	PS00205. 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]
ProtoNet	Search...
Other
NextBio	301824.
SOURCE	Search...

Entry information

Entry name

TRFE_MOUSE

Accession

Primary (citable) accession number: Q921I1
Secondary accession number(s): O35421 , 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:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program