TRFE_ANAPL
ID TRFE_ANAPL Reviewed; 686 AA.
AC P56410;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Ovotransferrin;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX PubMed=15299626; DOI=10.1107/s0907444996000212;
RA Rawas A., Muirhead H., Williams J.;
RT "Structure of diferric duck ovotransferrin at 2.35-A resolution.";
RL Acta Crystallogr. D 52:631-640(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).
RX PubMed=15299915; DOI=10.1107/s0907444997000838;
RA Rawas A., Muirhead H., Williams J.;
RT "Structure of apo duck ovotransferrin: the structures of the N and C lobes
RT are in the open form.";
RL Acta Crystallogr. D 53:464-468(1997).
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 -!- FUNCTION: Ovotransferrin has a bacteriostatic function. Its
CC concentration in avian egg is the highest concentration of any
CC transferrin in vivo (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR PDB; 1AOV; X-ray; 4.00 A; A=1-686.
DR PDB; 1DOT; X-ray; 2.35 A; A=1-686.
DR PDB; 1GV8; X-ray; 1.95 A; A=91-249.
DR PDB; 1GVC; X-ray; 1.90 A; A=91-247.
DR PDB; 1OVB; X-ray; 2.30 A; A=91-249.
DR PDBsum; 1AOV; -.
DR PDBsum; 1DOT; -.
DR PDBsum; 1GV8; -.
DR PDBsum; 1GVC; -.
DR PDBsum; 1OVB; -.
DR AlphaFoldDB; P56410; -.
DR PCDDB; P56410; -.
DR SMR; P56410; -.
DR Allergome; 2104; Ana p 3.
DR EvolutionaryTrace; P56410; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
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; 1.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Ion transport; Iron;
KW Iron transport; Metal-binding; Repeat; Secreted; Transport.
FT CHAIN 1..686
FT /note="Ovotransferrin"
FT /id="PRO_0000082440"
FT DOMAIN 7..333
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 345..670
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 333..341
FT /note="Connecting region"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 10..45
FT DISULFID 20..36
FT DISULFID 115..197
FT DISULFID 160..174
FT DISULFID 171..182
FT DISULFID 228..242
FT DISULFID 348..380
FT DISULFID 358..371
FT DISULFID 405..680
FT DISULFID 421..643
FT DISULFID 454..530
FT DISULFID 478..671
FT DISULFID 488..502
FT DISULFID 499..513
FT DISULFID 570..584
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 24..29
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1GVC"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1GVC"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1GVC"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1GV8"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1GVC"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1GVC"
FT TURN 178..182
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1OVB"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1GVC"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:1GVC"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1GVC"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1GVC"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1GVC"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 367..377
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 465..475
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 523..533
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 601..615
FT /evidence="ECO:0007829|PDB:1DOT"
FT TURN 620..624
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 631..634
FT /evidence="ECO:0007829|PDB:1DOT"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 653..657
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 659..668
FT /evidence="ECO:0007829|PDB:1DOT"
FT HELIX 675..683
FT /evidence="ECO:0007829|PDB:1DOT"
SQ SEQUENCE 686 AA; 75633 MW; 963FCF4727C3EBDD CRC64;
APPKTTVRWC TISSAEEKKC NSLKDHMQQE RVTLSCVQKA TYLDCIKAIS NNEADAISLD
GGQVFEAGLA PYKLKPIAAE VYERSGGSTT SYYAVAVVKK GTDFMIKDLR GKTSCHTGLG
RSAGWNIPIG TLIHREDIEW EGIESGISEQ AVAKFFSASC VPGATIEQKL CRQCKGDAKT
KCLRNGPYSG YSGAFQCLKD GKGDVAFVKH TTVQENAPEE KDEYELLCLD GSRQPVDSYK
TCNWARVAAH AVVARDDSKI DDIWSFLGMQ AYSLGVDTTS DFHLFGPPGK KDPVLKDLLF
KDSAIMLKRV PELMDSQLYL GFEYYSAIQS LRKDQLTVGP RENKIQWCAV GKDEKSKCDR
WSVVSNGEVE CTILDDNKDC IVKITKGEAD AISLDGGFVY TAGVCGLVPV VGESYEDETQ
CSKDEEQPAY YFAVAVVKKS SAITWNNLQG KKSCHTAVGR TAGWNIPMGL IHNKTGSCDF
DDYFSEGCAP GSPPNSRLCK LCQGSGENLL EKCVASSHEK YYGYTGALRC LVEQGDVAFI
KHSTVGENVS GSNKDDWAKG LTRDDFELLC TNGKRAKTMD YKTCHLAKVP THAVVARPEK
ANKIRELLEG QEKLFGLHGT EKERFMMFQS QTKDLLFKAL TKCLVKLRQG ITYKEFLGDE
YYASVASLNT CNPSDLLQVC TFLEDK
