ID G1L0E7_AILME Unreviewed; 709 AA.
AC G1L0E7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Serotransferrin {ECO:0000256|ARBA:ARBA00016768};
DE AltName: Full=Beta-1 metal-binding globulin {ECO:0000256|ARBA:ARBA00031058};
DE AltName: Full=Siderophilin {ECO:0000256|ARBA:ARBA00032359};
GN Name=TF {ECO:0000313|Ensembl:ENSAMEP00000000349.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000000349.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000000349.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000000349.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025170}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the transferrin family.
CC {ECO:0000256|PIRNR:PIRNR002549}.
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DR AlphaFoldDB; G1L0E7; -.
DR STRING; 9646.ENSAMEP00000000349; -.
DR Ensembl; ENSAMET00000000363.2; ENSAMEP00000000349.2; ENSAMEG00000000261.2.
DR eggNOG; KOG0090; Eukaryota.
DR GeneTree; ENSGT00940000154388; -.
DR HOGENOM; CLU_011309_1_0_1; -.
DR InParanoid; G1L0E7; -.
DR TreeFam; TF324013; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl.
DR GO; GO:0034986; F:iron chaperone activity; IEA:Ensembl.
DR GO; GO:1990459; F:transferrin receptor binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0071281; P:cellular response to iron ion; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0034756; P:regulation of iron ion transport; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd13617; PBP2_transferrin_C; 1.
DR CDD; cd13618; PBP2_transferrin_N; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR030685; Serotransferrin_mammal.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR PANTHER; PTHR11485:SF31; SEROTRANSFERRIN; 1.
DR PANTHER; PTHR11485; TRANSFERRIN; 1.
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 SUPFAM; SSF53850; Periplasmic binding protein-like II; 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron transport {ECO:0000256|ARBA:ARBA00022496};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..709
FT /note="Serotransferrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030170437"
FT DOMAIN 26..353
FT /note="Transferrin-like"
FT /evidence="ECO:0000259|PROSITE:PS51408"
FT DOMAIN 367..694
FT /note="Transferrin-like"
FT /evidence="ECO:0000259|PROSITE:PS51408"
SQ SEQUENCE 709 AA; 78763 MW; 279009BA4B8A9C23 CRC64;
MRLAVRALLA CAVLGLCLAV SPEKTVRWCT VSNHEASKCS SFMENMKTVL ENGPFVSCVK
KTSYLECIKA IWLNEADAVT LDAGLVFEAG LNPYNLKPVV AEFYGSEKDK QTHYYAVAVV
KKNSDFKLNE LQGKRSCHTG LGRSAGWNIP MGSLYWKLPE PRESLQKAAS NFFAGSCVPC
ADRTTFPKLC QLCLGKGTEK CACSNHEPYF GYSGAFKCLM DDAGEVAFVK HSTVFENLPN
EADWDNYRLL CPDNLHRMPV DKYKDCHLAS VPSHAVVARS VGGKEDLIWE LLNQAQEHYG
KDKSKVFQLF SSTLGKDLLF KDSAQGFLKI PPKMDTWLYL GYDYVTALRN LREDVRPDTP
RDECKKVKWC AIGHHERVKC DEWSVNSEGK IECESAESTE DCIAKIAKGE ADAMSLDGGF
IYIAGKCGLV PVLAENYKTE GPDCSNTAEE GYRAVAVVKA SADDTLTWNN LRGRKSCHTA
VDRTAGWNIP MGLLYSRINN CEFDKFFEEG CAPGSMRNSS LCALCIGSAN VPGKECVPNN
HERYYGYTGA FRCLVEKGDV AFVKDQTVMQ NTEGRNTEDW AKNLKEENFR LLCPDGQRKP
VSEAKNCFLA QAPNHAVVSR KDKASCVSKL LLEQQLLFGG SGNDCSGKFC LFHSETKDLL
FRDDTKCLAK LPDGTTYESY LGADYVRAVS NLRQCSTSKL LEACTFHRL
//
