TRFE_PIG
ID TRFE_PIG Reviewed; 696 AA.
AC P09571;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Serotransferrin;
DE Short=Transferrin;
DE AltName: Full=Beta-1 metal-binding globulin;
DE AltName: Full=Siderophilin;
GN Name=TF;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3419934; DOI=10.1093/nar/16.17.8720;
RA Baldwin G.S., Weinstock J.;
RT "Nucleotide sequence of porcine liver transferrin.";
RL Nucleic Acids Res. 16:8720-8720(1988).
RN [2]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=2065820;
RA Chung M.C., Chan S.L., Shimizu S.;
RT "Purification of transferrins and lactoferrin using DEAE affi-gel blue.";
RL Int. J. Biochem. 23:609-616(1991).
RN [3]
RP PROTEIN SEQUENCE OF 1-15.
RX PubMed=2328566; DOI=10.1016/0305-0491(90)90074-4;
RA Baldwin G.S., Bacic T., Chandler R., Grego B., Pedersen J., Simpson R.J.,
RA Toh B.H., Weinstock J.;
RT "Isolation of transferrin from porcine gastric mucosa: comparison with
RT porcine serum transferrin.";
RL Comp. Biochem. Physiol. 95B:261-268(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX PubMed=11752780; DOI=10.1107/s0907444901017309;
RA Hall D.R., Hadden J.M., Leonard G.A., Bailey S., Neu M., Winn M.,
RA Lindley P.F.;
RT "The crystal and molecular structures of diferric porcine and rabbit serum
RT transferrins at resolutions of 2.15 and 2.60 A, respectively.";
RL Acta Crystallogr. D 58:70-80(2002).
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; X12386; CAA30943.1; -; mRNA.
DR PIR; S01384; S01384.
DR PDB; 1H76; X-ray; 2.15 A; A=1-696.
DR PDBsum; 1H76; -.
DR AlphaFoldDB; P09571; -.
DR SMR; P09571; -.
DR STRING; 9823.ENSSSCP00000012406; -.
DR MEROPS; S60.970; -.
DR PaxDb; P09571; -.
DR PeptideAtlas; P09571; -.
DR PRIDE; P09571; -.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR InParanoid; P09571; -.
DR EvolutionaryTrace; P09571; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
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; 2.
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; Transport.
FT CHAIN 1..696
FT /note="Serotransferrin"
FT /id="PRO_0000082439"
FT DOMAIN 6..332
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 346..672
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 62
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 94
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 119
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 123
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 125
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 126
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 192
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 253
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 396
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 431
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 458
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 462
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 464
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 465
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 526
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 594
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT MOD_RES 23
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P12346"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 9..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 19..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 117..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 157..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 160..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 170..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 231..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 343..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 349..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 359..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 406..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 423..646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 456..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 480..673
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 490..504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 501..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 572..586
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 624..629
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT VARIANT 308
FT /note="K -> R"
FT CONFLICT 20
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:1H76"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1H76"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1H76"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:1H76"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 409..417
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:1H76"
FT TURN 463..466
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 467..477
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 525..535
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:1H76"
FT TURN 558..562
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 580..585
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 603..617
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 634..637
FT /evidence="ECO:0007829|PDB:1H76"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 655..659
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 661..669
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:1H76"
FT HELIX 677..682
FT /evidence="ECO:0007829|PDB:1H76"
SQ SEQUENCE 696 AA; 76968 MW; 787C59F42D844B26 CRC64;
VAQKTVRWCT ISNQEANKCS SFRENMSKAV KNGPLVSCVK KSSYLDCIKA IRDKEADAVT
LDAGLVFEAG LAPYNLKPVV AEFYGQKDNP QTHYYAVAVV KKGSNFQWNQ LQGKRSCHTG
LGRSAGWIIP MGLLYDQLPE PRKPIEKAVA SFFSSSCVPC ADPVNFPKLC QQCAGKGAEK
CACSNHEPYF GYAGAFNCLK EDAGDVAFVK HSTVLENLPD KADRDQYELL CRDNTRRPVD
DYENCYLAQV PSHAVVARSV DGQEDSIWEL LNQAQEHFGR DKSPDFQLFS SSHGKDLLFK
DSANGFLKIP SKMDSSLYLG YQYVTALRNL REEISPDSSK NECKKVRWCA IGHEETQKCD
AWSINSGGKI ECVSAENTED CIAKIVKGEA DAMSLDGGYI YIAGKCGLVP VLAENYKTEG
ENCVNTPEKG YLAVAVVKKS SGPDLNWNNL KGKKSCHTAV DRTAGWNIPM GLLYNKINSC
KFDQFFGEGC APGSQRNSSL CALCIGSERA PGRECLANNH ERYYGYTGAF RCLVEKGDVA
FVKDQVVQQN TDGKNKDDWA KDLKQMDFEL LCQNGAREPV DNAENCHLAR APNHAVVARD
DKVTCVAEEL LKQQAQFGRH VTDCSSSFCM FKSNTKDLLF RDDTQCLARV GKTTYESYLG
ADYITAVANL RKCSTSKLLE ACTFHSAKNP RVETTT
