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Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Liver regeneration-related protein LRRG03) (Siderophilin)

 TRFE_RAT                Reviewed;         698 AA.
P12346; Q63602; Q64628; Q64630; Q7TNX0;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 3.
07-JUN-2017, entry version 154.
RecName: Full=Serotransferrin;
Short=Transferrin;
AltName: Full=Beta-1 metal-binding globulin;
AltName: Full=Liver regeneration-related protein LRRG03;
AltName: Full=Siderophilin;
Flags: Precursor;
Name=Tf;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Wistar; TISSUE=Mammary gland;
PubMed=7717992; DOI=10.1042/bj3070047;
Escriva H., Pierce A., Coddeville B., Gonzalez F., Benaissa M.,
Leger D., Wieruszeski J.-M., Spik G., Pamblanco M.;
"Rat mammary-gland transferrin: nucleotide sequence, phylogenetic
analysis and glycan structure.";
Biochem. J. 307:47-55(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Wistar; TISSUE=Liver;
PubMed=8829802; DOI=10.1016/0305-0491(95)02068-3;
Hosino A., Hisayasu S., Shimada T.;
"Complete sequence analysis of rat transferrin and expression of
transferrin but not lactoferrin in the digestive glands.";
Comp. Biochem. Physiol. 113B:491-497(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
"Liver regeneration after PH.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-295 (ISOFORM 2).
PubMed=6236811; DOI=10.1016/0006-291X(84)91185-9;
Aldred A.R., Howlett G.J., Schreiber G.;
"Synthesis of rat transferrin in Escherichia coli containing a
recombinant bacteriophage.";
Biochem. Biophys. Res. Commun. 122:960-965(1984).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 521-698.
PubMed=3023031; DOI=10.1210/endo-120-1-332;
Huggenvik J.I., Idzerda R.L., Haywood L., Lee D.C., McKnight G.S.,
Griswold M.D.;
"Transferrin messenger ribonucleic acid: molecular cloning and
hormonal regulation in rat Sertoli cells.";
Endocrinology 120:332-340(1987).
[7]
PROTEIN SEQUENCE OF 20-47.
PubMed=500689;
Schreiber G., Dryburgh H., Millership A., Matsuda Y., Inglis A.,
Phillips J., Edwards K., Maggs J.;
"The synthesis and secretion of rat transferrin.";
J. Biol. Chem. 254:12013-12019(1979).
[8]
PROTEIN SEQUENCE OF 20-30 AND 642-653.
PubMed=3046665; DOI=10.1016/0304-4165(88)90081-5;
Purves L.R., Purves M., Linton N., Brandt W., Johnson G., Jacobs P.;
"Properties of the transferrin associated with rat intestinal
mucosa.";
Biochim. Biophys. Acta 966:318-327(1988).
[9]
PROTEIN SEQUENCE OF 89-102; 232-243 AND 404-411.
PubMed=1791188; DOI=10.1002/jcb.240470312;
Cavanaugh P.G., Nicolson G.L.;
"Lung-derived growth factor that stimulates the growth of lung-
metastasizing tumor cells: identification as transferrin.";
J. Cell. Biochem. 47:261-271(1991).
[10]
PROTEIN SEQUENCE OF 144-162; 240-251; 332-343; 588-609; 616-624;
630-642 AND 660-682, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[11]
METHYLATION AT ARG-42, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15047867; DOI=10.1091/mbc.E04-02-0101;
Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
Yates J.R. III, Howell K.E.;
"Organellar proteomics reveals Golgi arginine dimethylation.";
Mol. Biol. Cell 15:2907-2919(2004).
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) 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: Monomer.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P12346-1; Sequence=Displayed;
Name=2;
IsoId=P12346-2; Sequence=VSP_011840;
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X77158; CAA54403.1; -; mRNA.
EMBL; D38380; BAA07458.1; -; mRNA.
EMBL; AY327504; AAP97736.1; -; mRNA.
EMBL; BC087021; AAH87021.1; -; mRNA.
EMBL; M26113; AAA42266.1; -; mRNA.
EMBL; M27966; AAA42267.1; -; mRNA.
PIR; S49163; S49163.
RefSeq; NP_001013128.1; NM_001013110.1. [P12346-1]
UniGene; Rn.91296; -.
ProteinModelPortal; P12346; -.
SMR; P12346; -.
BioGrid; 246945; 1.
IntAct; P12346; 1.
MINT; MINT-246684; -.
STRING; 10116.ENSRNOP00000012725; -.
Allergome; 1417; Rat n Transferrin.
MEROPS; S60.970; -.
iPTMnet; P12346; -.
PhosphoSitePlus; P12346; -.
UniCarbKB; P12346; -.
World-2DPAGE; 0004:P12346; -.
PaxDb; P12346; -.
PRIDE; P12346; -.
Ensembl; ENSRNOT00000045628; ENSRNOP00000045637; ENSRNOG00000030625. [P12346-1]
GeneID; 24825; -.
KEGG; rno:24825; -.
UCSC; RGD:3845; rat. [P12346-1]
CTD; 7018; -.
RGD; 3845; Tf.
eggNOG; ENOG410IEAI; Eukaryota.
eggNOG; ENOG410XQ36; LUCA.
GeneTree; ENSGT00390000001619; -.
HOGENOM; HOG000043759; -.
HOVERGEN; HBG000055; -.
InParanoid; P12346; -.
KO; K14736; -.
PhylomeDB; P12346; -.
Reactome; R-RNO-114608; Platelet degranulation.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
Reactome; R-RNO-917937; Iron uptake and transport.
Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
PRO; PR:P12346; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000030625; -.
ExpressionAtlas; P12346; baseline and differential.
Genevisible; P12346; RN.
GO; GO:0005604; C:basement membrane; IDA:RGD.
GO; GO:0051286; C:cell tip; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0008199; F:ferric iron binding; IDA:RGD.
GO; GO:0015091; F:ferric iron transmembrane transporter activity; IEA:InterPro.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:UniProtKB.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:UniProtKB.
GO; GO:0015682; P:ferric iron transport; IDA:RGD.
GO; GO:0006826; P:iron ion transport; TAS:RGD.
GO; GO:0031643; P:positive regulation of myelination; IDA:RGD.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
InterPro; IPR030685; Serotransferrin_mammal.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF500682; Serotransferrin; 1.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport;
Metal-binding; Methylation; Phosphoprotein; Reference proteome;
Repeat; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:3046665,
ECO:0000269|PubMed:500689}.
CHAIN 20 698 Serotransferrin.
/FTId=PRO_0000035718.
DOMAIN 25 347 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 360 683 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 82 82 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 114 114 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 207 207 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 268 268 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 410 410 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 447 447 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 536 536 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 604 604 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 139 139 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 143 143 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 145 145 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 146 146 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 473 473 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 477 477 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 479 479 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 480 480 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
MOD_RES 42 42 Dimethylated arginine.
{ECO:0000269|PubMed:15047867}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
MOD_RES 685 685 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
CARBOHYD 512 512 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 67 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 38 58 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 137 213 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 156 350 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 177 193 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 180 196 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 190 198 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 246 260 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 363 395 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 373 386 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 420 693 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 435 656 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 471 542 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 495 684 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 505 519 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 516 525 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 582 596 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 634 639 {ECO:0000255|PROSITE-ProRule:PRU00741}.
VAR_SEQ 65 266 Missing (in isoform 2).
{ECO:0000303|PubMed:6236811}.
/FTId=VSP_011840.
CONFLICT 57 57 A -> P (in Ref. 1; CAA54403).
{ECO:0000305}.
CONFLICT 110 110 P -> R (in Ref. 1; CAA54403).
{ECO:0000305}.
CONFLICT 318 318 A -> R (in Ref. 1; CAA54403).
{ECO:0000305}.
CONFLICT 321 323 LLR -> CYG (in Ref. 2; BAA07458).
{ECO:0000305}.
CONFLICT 324 354 VPPRMDYRLYLGHSYVTAIRNQREGVCPEGS -> APKDGL
QAVPRPQLCHCHSKSAGSCPDA (in Ref. 1;
CAA54403). {ECO:0000305}.
CONFLICT 353 353 G -> A (in Ref. 2; BAA07458).
{ECO:0000305}.
CONFLICT 379 379 S -> T (in Ref. 1; CAA54403 and 2;
BAA07458). {ECO:0000305}.
CONFLICT 380 380 S -> G (in Ref. 1; CAA54403).
{ECO:0000305}.
CONFLICT 691 691 E -> D (in Ref. 6; AAA42267).
{ECO:0000305}.
CONFLICT 696 697 HK -> TA (in Ref. 6; AAA42267).
{ECO:0000305}.
SEQUENCE 698 AA; 76395 MW; B91ABB41CA447194 CRC64;
MRFAVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP ADGPRLACVK
KTSYQDCIKA ISGGEADAIT LDGGWVYDAG LTPNNLKPVA AEFYGSLEHP QTHYLAVAVV
KKGTDFQLNQ LQGKKSCHTG LGRSAGWIIP IGLLFCNLPE PRKPLEKAVA SFFSGSCVPC
ADPVAFPQLC QLCPGCGCSP TQPFFGYVGA FKCLRDGGGD VAFVKHTTIF EVLPQKADRD
QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARNGDGKED LIWEILKVAQ EHFGKGKSKD
FQLFGSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHSYVT AIRNQREGVC PEGSIDSAPV
KWCALSHQER AKCDEWSVSS NGQIECESAE STEDCIDKIV NGEADAMSLD GGHAYIAGQC
GLVPVMAENY DISSCTNPQS DVFPKGYYAV AVVKASDSSI NWNNLKGKKS CHTGVDRTAG
WNIPMGLLFS RINHCKFDEF FSQGCAPGYK KNSTLCDLCI GPAKCAPNNR EGYNGYTGAF
QCLVEKGDVA FVKHQTVLEN TNGKNTAAWA KDLKQEDFQL LCPDGTKKPV TEFATCHLAQ
APNHVVVSRK EKAARVSTVL TAQKDLFWKG DKDCTGNFCL FRSSTKDLLF RDDTKCLTKL
PEGTTYEEYL GAEYLQAVGN IRKCSTSRLL EACTFHKS


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