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Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Siderophilin)

 TRFE_RABIT              Reviewed;         695 AA.
P19134; O46514;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 4.
10-MAY-2017, entry version 124.
RecName: Full=Serotransferrin;
Short=Transferrin;
AltName: Full=Beta-1 metal-binding globulin;
AltName: Full=Siderophilin;
Flags: Precursor;
Name=TF;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2054387; DOI=10.1016/0167-4781(91)90021-D;
Banfield D.K., Chow B.K.-C., Funk W.D., Robertson K.A., Umelas T.M.,
Woodworth R.C., Macgillivray R.T.A.;
"The nucleotide sequence of rabbit liver transferrin cDNA.";
Biochim. Biophys. Acta 1089:262-265(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=New Zealand white;
Ghareeb B.A.A., Thepot D., Puissant C., Cajero-Juaerez M.,
Houdebine L.-M.;
"Cloning and structural organisation of the rabbit transferrin
encoding gene.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 20-51.
PubMed=3365331;
Godovac-Zimmermann J.;
"Isolation, characterization and N-terminal amino-acid sequence of
rabbit transferrin.";
Biol. Chem. Hoppe-Seyler 369:93-96(1988).
[4]
PROTEIN SEQUENCE OF 483-545.
PubMed=3169252; DOI=10.1016/0014-5793(88)80221-7;
Evans R.W., Aitken A., Patel K.J.;
"Evidence for a single glycan moiety in rabbit serum transferrin and
location of the glycan within the polypeptide chain.";
FEBS Lett. 238:39-42(1988).
[5]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
TISSUE=Plasma;
PubMed=3179277; DOI=10.1021/bi00415a061;
Bailey S., Evans R.W., Garratt R.C., Gorinsky B., Hasnain S.,
Horsburgh C., Jhoti H., Lindley P.F., Mydin A., Sarra R., Watson J.L.;
"Molecular structure of serum transferrin at 3.3-A resolution.";
Biochemistry 27:5804-5812(1988).
[6]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Sarra R., Garratt R.C., Gorinsky B., Jhoti H., Lindley P.F.;
"High-resolution X-ray studies on rabbit serum transferrin:
preliminary structure analysis of the N-terminal half-molecule at 2.3-
A resolution.";
Acta Crystallogr. B 46:763-771(1990).
-!- 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.
-!- 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; X58533; CAA41424.1; -; mRNA.
EMBL; AF031625; AAB94136.1; -; Genomic_DNA.
EMBL; AF031611; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031612; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031613; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031614; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031615; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031616; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031617; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031618; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031619; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031620; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031621; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031622; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031623; AAB94136.1; JOINED; Genomic_DNA.
EMBL; AF031624; AAB94136.1; JOINED; Genomic_DNA.
PIR; S16246; TFRBP.
RefSeq; NP_001095164.1; NM_001101694.1.
UniGene; Ocu.6256; -.
PDB; 1JNF; X-ray; 2.60 A; A=20-695.
PDB; 1TFD; X-ray; 2.30 A; A=20-323.
PDBsum; 1JNF; -.
PDBsum; 1TFD; -.
ProteinModelPortal; P19134; -.
SMR; P19134; -.
STRING; 9986.ENSOCUP00000006587; -.
MEROPS; S60.972; -.
PRIDE; P19134; -.
GeneID; 100009267; -.
KEGG; ocu:100009267; -.
CTD; 7018; -.
eggNOG; ENOG410IEAI; Eukaryota.
eggNOG; ENOG410XQ36; LUCA.
HOGENOM; HOG000043759; -.
HOVERGEN; HBG000055; -.
InParanoid; P19134; -.
KO; K14736; -.
EvolutionaryTrace; P19134; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0015091; F:ferric iron transmembrane transporter activity; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
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;
3D-structure; 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:3365331}.
CHAIN 20 695 Serotransferrin.
/FTId=PRO_0000035717.
DOMAIN 25 347 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 361 680 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 82 82 Iron 1.
METAL 114 114 Iron 1.
METAL 207 207 Iron 1.
METAL 268 268 Iron 1.
METAL 411 411 Iron 2.
METAL 444 444 Iron 2.
METAL 533 533 Iron 2.
METAL 601 601 Iron 2.
BINDING 139 139 Carbonate 1.
BINDING 143 143 Carbonate 1.
BINDING 145 145 Carbonate 1; via amide nitrogen.
BINDING 146 146 Carbonate 1; via amide nitrogen.
BINDING 470 470 Carbonate 2.
BINDING 474 474 Carbonate 2.
BINDING 476 476 Carbonate 2; via amide nitrogen.
BINDING 477 477 Carbonate 2; via amide nitrogen.
MOD_RES 42 42 Dimethylated arginine.
{ECO:0000250|UniProtKB:P12346}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
CARBOHYD 509 509 N-linked (GlcNAc...) asparagine.
DISULFID 28 67
DISULFID 38 58
DISULFID 137 213
DISULFID 156 350
DISULFID 177 193
DISULFID 180 196
DISULFID 190 198
DISULFID 246 260
DISULFID 358 612
DISULFID 364 396
DISULFID 374 387
DISULFID 421 690
DISULFID 436 653
DISULFID 468 539
DISULFID 492 681
DISULFID 502 516
DISULFID 513 522
DISULFID 579 593
DISULFID 631 636
VARIANT 517 517 V -> I.
CONFLICT 7 7 Missing (in Ref. 1; CAA41424).
{ECO:0000305}.
CONFLICT 47 47 K -> S (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 50 50 P -> Y (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 27 29 {ECO:0000244|PDB:1TFD}.
HELIX 32 45 {ECO:0000244|PDB:1TFD}.
TURN 46 48 {ECO:0000244|PDB:1TFD}.
STRAND 51 53 {ECO:0000244|PDB:1TFD}.
STRAND 55 63 {ECO:0000244|PDB:1JNF}.
HELIX 64 72 {ECO:0000244|PDB:1TFD}.
STRAND 78 81 {ECO:0000244|PDB:1TFD}.
HELIX 83 90 {ECO:0000244|PDB:1TFD}.
TURN 91 94 {ECO:0000244|PDB:1TFD}.
STRAND 96 102 {ECO:0000244|PDB:1TFD}.
STRAND 107 109 {ECO:0000244|PDB:1TFD}.
STRAND 114 121 {ECO:0000244|PDB:1TFD}.
HELIX 128 130 {ECO:0000244|PDB:1JNF}.
STRAND 136 139 {ECO:0000244|PDB:1JNF}.
TURN 144 147 {ECO:0000244|PDB:1TFD}.
HELIX 148 154 {ECO:0000244|PDB:1TFD}.
TURN 155 157 {ECO:0000244|PDB:1TFD}.
HELIX 165 170 {ECO:0000244|PDB:1TFD}.
STRAND 173 177 {ECO:0000244|PDB:1TFD}.
TURN 183 185 {ECO:0000244|PDB:1JNF}.
STRAND 190 193 {ECO:0000244|PDB:1TFD}.
STRAND 198 200 {ECO:0000244|PDB:1TFD}.
STRAND 202 206 {ECO:0000244|PDB:1TFD}.
HELIX 207 214 {ECO:0000244|PDB:1TFD}.
TURN 215 217 {ECO:0000244|PDB:1TFD}.
STRAND 218 225 {ECO:0000244|PDB:1TFD}.
HELIX 228 232 {ECO:0000244|PDB:1TFD}.
HELIX 236 239 {ECO:0000244|PDB:1TFD}.
STRAND 242 246 {ECO:0000244|PDB:1TFD}.
TURN 247 249 {ECO:0000244|PDB:1TFD}.
STRAND 250 253 {ECO:0000244|PDB:1TFD}.
HELIX 254 256 {ECO:0000244|PDB:1JNF}.
TURN 257 259 {ECO:0000244|PDB:1TFD}.
STRAND 262 265 {ECO:0000244|PDB:1TFD}.
STRAND 269 276 {ECO:0000244|PDB:1TFD}.
HELIX 279 288 {ECO:0000244|PDB:1TFD}.
TURN 289 291 {ECO:0000244|PDB:1TFD}.
STRAND 292 296 {ECO:0000244|PDB:1TFD}.
STRAND 309 311 {ECO:0000244|PDB:1TFD}.
STRAND 320 323 {ECO:0000244|PDB:1JNF}.
HELIX 330 334 {ECO:0000244|PDB:1JNF}.
HELIX 336 346 {ECO:0000244|PDB:1JNF}.
STRAND 361 366 {ECO:0000244|PDB:1JNF}.
HELIX 368 381 {ECO:0000244|PDB:1JNF}.
STRAND 382 392 {ECO:0000244|PDB:1JNF}.
HELIX 393 401 {ECO:0000244|PDB:1JNF}.
STRAND 407 410 {ECO:0000244|PDB:1JNF}.
HELIX 412 420 {ECO:0000244|PDB:1JNF}.
STRAND 424 430 {ECO:0000244|PDB:1JNF}.
STRAND 444 453 {ECO:0000244|PDB:1JNF}.
HELIX 459 461 {ECO:0000244|PDB:1JNF}.
STRAND 465 470 {ECO:0000244|PDB:1JNF}.
TURN 475 478 {ECO:0000244|PDB:1JNF}.
HELIX 479 489 {ECO:0000244|PDB:1JNF}.
HELIX 494 497 {ECO:0000244|PDB:1JNF}.
STRAND 498 502 {ECO:0000244|PDB:1JNF}.
HELIX 511 513 {ECO:0000244|PDB:1JNF}.
STRAND 518 520 {ECO:0000244|PDB:1JNF}.
HELIX 532 542 {ECO:0000244|PDB:1JNF}.
STRAND 545 550 {ECO:0000244|PDB:1JNF}.
HELIX 553 557 {ECO:0000244|PDB:1JNF}.
TURN 565 569 {ECO:0000244|PDB:1JNF}.
HELIX 572 574 {ECO:0000244|PDB:1JNF}.
STRAND 575 578 {ECO:0000244|PDB:1JNF}.
STRAND 584 586 {ECO:0000244|PDB:1JNF}.
HELIX 587 592 {ECO:0000244|PDB:1JNF}.
STRAND 595 598 {ECO:0000244|PDB:1JNF}.
STRAND 602 605 {ECO:0000244|PDB:1JNF}.
TURN 607 609 {ECO:0000244|PDB:1JNF}.
HELIX 610 624 {ECO:0000244|PDB:1JNF}.
TURN 631 633 {ECO:0000244|PDB:1JNF}.
STRAND 641 643 {ECO:0000244|PDB:1JNF}.
STRAND 645 647 {ECO:0000244|PDB:1JNF}.
STRAND 653 656 {ECO:0000244|PDB:1JNF}.
HELIX 663 667 {ECO:0000244|PDB:1JNF}.
HELIX 669 677 {ECO:0000244|PDB:1JNF}.
HELIX 678 681 {ECO:0000244|PDB:1JNF}.
HELIX 685 690 {ECO:0000244|PDB:1JNF}.
SEQUENCE 695 AA; 76670 MW; DB12F34D87AE9D55 CRC64;
MRLAAGALLA CAALGLCLAV TEKTVRWCAV NDHEASKCAN FRDSMKKVLP EDGPRIICVK
KASYLDCIKA IAAHEADAVT LDAGLVHEAG LTPNNLKPVV AEFYGSKENP KTFYYAVALV
KKGSNFQLNE LQGKKSCHTG LGRSAGWNIP IGLLYCDLPE PRKPLEKAVA SFFSGSCVPC
ADGADFPQLC QLCPGCGCSS VQPYFGYSGA FKCLKDGLGD VAFVKQETIF ENLPSKDERD
QYELLCLDNT RKPVDEYEQC HLARVPSHAV VARSVDGKED LIWELLNQAQ EHFGKDKSGD
FQLFSSPHGK NLLFKDSAYG FFKVPPRMDA NLYLGYEYVT AVRNLREGIC PDPLQDECKA
VKWCALSHHE RLKCDEWSVT SGGLIECESA ETPEDCIAKI MNGEADAMSL DGGYVYIAGQ
CGLVPVLAEN YESTDCKKAP EEGYLSVAVV KKSNPDINWN NLEGKKSCHT AVDRTAGWNI
PMGLLYNRIN HCRFDEFFRQ GCAPGSQKNS SLCELCVGPS VCAPNNREGY YGYTGAFRCL
VEKGDVAFVK SQTVLQNTGG RNSEPWAKDL KEEDFELLCL DGTRKPVSEA HNCHLAKAPN
HAVVSRKDKA ACVKQKLLDL QVEYGNTVAD CSSKFCMFHS KTKDLLFRDD TKCLVDLRGK
NTYEKYLGAD YIKAVSNLRK CSTSRLLEAC TFHKH


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