TRFE_RABIT
ID TRFE_RABIT Reviewed; 695 AA.
AC P19134; O46514;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 4.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serotransferrin;
DE Short=Transferrin;
DE AltName: Full=Beta-1 metal-binding globulin;
DE AltName: Full=Siderophilin;
DE Flags: Precursor;
GN Name=TF;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2054387; DOI=10.1016/0167-4781(91)90021-d;
RA Banfield D.K., Chow B.K.-C., Funk W.D., Robertson K.A., Umelas T.M.,
RA Woodworth R.C., Macgillivray R.T.A.;
RT "The nucleotide sequence of rabbit liver transferrin cDNA.";
RL Biochim. Biophys. Acta 1089:262-265(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=New Zealand white;
RA Ghareeb B.A.A., Thepot D., Puissant C., Cajero-Juaerez M., Houdebine L.-M.;
RT "Cloning and structural organisation of the rabbit transferrin encoding
RT gene.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 20-51.
RX PubMed=3365331; DOI=10.1515/bchm3.1988.369.1.93;
RA Godovac-Zimmermann J.;
RT "Isolation, characterization and N-terminal amino-acid sequence of rabbit
RT transferrin.";
RL Biol. Chem. Hoppe-Seyler 369:93-96(1988).
RN [4]
RP PROTEIN SEQUENCE OF 483-545.
RX PubMed=3169252; DOI=10.1016/0014-5793(88)80221-7;
RA Evans R.W., Aitken A., Patel K.J.;
RT "Evidence for a single glycan moiety in rabbit serum transferrin and
RT location of the glycan within the polypeptide chain.";
RL FEBS Lett. 238:39-42(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RC TISSUE=Plasma;
RX PubMed=3179277; DOI=10.1021/bi00415a061;
RA Bailey S., Evans R.W., Garratt R.C., Gorinsky B., Hasnain S., Horsburgh C.,
RA Jhoti H., Lindley P.F., Mydin A., Sarra R., Watson J.L.;
RT "Molecular structure of serum transferrin at 3.3-A resolution.";
RL Biochemistry 27:5804-5812(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RA Sarra R., Garratt R.C., Gorinsky B., Jhoti H., Lindley P.F.;
RT "High-resolution X-ray studies on rabbit serum transferrin: preliminary
RT structure analysis of the N-terminal half-molecule at 2.3-A resolution.";
RL Acta Crystallogr. B 46:763-771(1990).
CC -!- FUNCTION: Transferrins are iron binding transport proteins which can
CC bind two Fe(3+) ions in association with the binding of an anion,
CC usually bicarbonate. It is responsible for the transport of iron from
CC sites of absorption and heme degradation to those of storage and
CC utilization. Serum transferrin may also have a further role in
CC stimulating cell proliferation.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; X58533; CAA41424.1; -; mRNA.
DR EMBL; AF031625; AAB94136.1; -; Genomic_DNA.
DR EMBL; AF031611; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031612; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031613; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031614; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031615; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031616; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031617; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031618; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031619; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031620; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031621; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031622; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031623; AAB94136.1; JOINED; Genomic_DNA.
DR EMBL; AF031624; AAB94136.1; JOINED; Genomic_DNA.
DR PIR; S16246; TFRBP.
DR RefSeq; NP_001095164.1; NM_001101694.1.
DR PDB; 1JNF; X-ray; 2.60 A; A=20-695.
DR PDB; 1TFD; X-ray; 2.30 A; A=20-323.
DR PDBsum; 1JNF; -.
DR PDBsum; 1TFD; -.
DR AlphaFoldDB; P19134; -.
DR SMR; P19134; -.
DR STRING; 9986.ENSOCUP00000006587; -.
DR MEROPS; S60.972; -.
DR PRIDE; P19134; -.
DR GeneID; 100009267; -.
DR KEGG; ocu:100009267; -.
DR CTD; 7018; -.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR InParanoid; P19134; -.
DR OrthoDB; 232859at2759; -.
DR EvolutionaryTrace; P19134; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR InterPro; IPR030685; Serotransferrin_mammal.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF500682; Serotransferrin; 1.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Ion transport; Iron; Iron transport; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3365331"
FT CHAIN 20..695
FT /note="Serotransferrin"
FT /id="PRO_0000035717"
FT DOMAIN 25..347
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 361..680
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 82
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 114
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 139
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 145
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 146
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 207
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 268
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 411
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT BINDING 444
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT BINDING 470
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 474
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 476
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 477
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 533
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT BINDING 601
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT MOD_RES 42
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P12346"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 28..67
FT DISULFID 38..58
FT DISULFID 137..213
FT DISULFID 156..350
FT DISULFID 177..193
FT DISULFID 180..196
FT DISULFID 190..198
FT DISULFID 246..260
FT DISULFID 358..612
FT DISULFID 364..396
FT DISULFID 374..387
FT DISULFID 421..690
FT DISULFID 436..653
FT DISULFID 468..539
FT DISULFID 492..681
FT DISULFID 502..516
FT DISULFID 513..522
FT DISULFID 579..593
FT DISULFID 631..636
FT VARIANT 517
FT /note="V -> I"
FT CONFLICT 7
FT /note="Missing (in Ref. 1; CAA41424)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="K -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="P -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1TFD"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1TFD"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1JNF"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:1TFD"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1TFD"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:1TFD"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1TFD"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1JNF"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1TFD"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:1TFD"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1TFD"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 382..392
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 393..401
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 412..420
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 444..453
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:1JNF"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 479..489
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 532..542
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 553..557
FT /evidence="ECO:0007829|PDB:1JNF"
FT TURN 565..569
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 587..592
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:1JNF"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 610..624
FT /evidence="ECO:0007829|PDB:1JNF"
FT TURN 631..633
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:1JNF"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 663..667
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 669..677
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 678..681
FT /evidence="ECO:0007829|PDB:1JNF"
FT HELIX 685..690
FT /evidence="ECO:0007829|PDB:1JNF"
SQ 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
