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Alpha-fetoprotein (Alpha-1-fetoprotein) (Alpha-fetoglobulin)

 FETA_HUMAN              Reviewed;         609 AA.
P02771; B2RBU3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-JUL-2017, entry version 180.
RecName: Full=Alpha-fetoprotein;
AltName: Full=Alpha-1-fetoprotein;
AltName: Full=Alpha-fetoglobulin;
Flags: Precursor;
Name=AFP; Synonyms=HPAFP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6192439; DOI=10.1073/pnas.80.15.4604;
Morinaga T., Sakai M., Wegmann T.G., Tamaoki T.;
"Primary structures of human alpha-fetoprotein and its mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:4604-4608(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2436661; DOI=10.1021/bi00379a020;
Gibbs P.E.M., Zielinski R., Boyd C., Dugaiczyk A.;
"Structure, polymorphism, and novel repeated DNA elements revealed by
a complete sequence of the human alpha-fetoprotein gene.";
Biochemistry 26:1332-1343(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-570.
TISSUE=Heart;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 AND 596-609, AND GENE
STRUCTURE.
PubMed=2580830;
Sakai M., Morinaga T., Urano Y., Watanabe K., Wegmann T.G.,
Tamaoki T.;
"The human alpha-fetoprotein gene. Sequence organization and the 5'
flanking region.";
J. Biol. Chem. 260:5055-5060(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND INVOLVEMENT IN HPAFP.
PubMed=7684942; DOI=10.1093/hmg/2.4.379;
McVey J.H., Michaelides K., Hansen L.P., Ferguson-Smith M.,
Tilghman S., Krumlauf R., Tuddenham E.G.D.;
"A G-->A substitution in an HNF I binding site in the human alpha-
fetoprotein gene is associated with hereditary persistence of alpha-
fetoprotein (HPAFP).";
Hum. Mol. Genet. 2:379-384(1993).
[7]
PROTEIN SEQUENCE OF 311-332; 348-372 AND 422-437, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 429-556.
PubMed=6187626; DOI=10.1016/0378-1119(82)90210-4;
Beattie W.G., Dugaiczyk A.;
"Structure and evolution of human alpha-fetoprotein deduced from
partial sequence of cloned cDNA.";
Gene 20:415-422(1982).
[9]
PROTEIN SEQUENCE OF 19-609.
PubMed=1709810; DOI=10.1021/bi00234a032;
Pucci P., Siciliano R., Malorni A., Marino G., Tecce M.F.,
Ceccarini C., Terrana B.;
"Human alpha-fetoprotein primary structure: a mass spectrometric
study.";
Biochemistry 30:5061-5066(1991).
[10]
PRELIMINARY PROTEIN SEQUENCE OF 19-35.
PubMed=70228; DOI=10.1016/0005-2795(77)90198-2;
Yachnin S., Hsu R., Heinrikson R.L., Miller J.B.;
"Studies on human alpha-fetoprotein. Isolation and characterization of
monomeric and polymeric forms and amino-terminal sequence analysis.";
Biochim. Biophys. Acta 493:418-428(1977).
[11]
PRELIMINARY PROTEIN SEQUENCE OF 19-38.
PubMed=71198;
Aoyagi Y., Ikenaka T., Ichida F.;
"Comparative chemical structures of human alpha-fetoproteins from
fetal serum and from ascites fluid of a patient with hepatoma.";
Cancer Res. 37:3663-3667(1977).
[12]
PRELIMINARY PROTEIN SEQUENCE OF 19-39.
PubMed=4138095;
Ruoslahti E., Pihko H., Vaheri A., Seppala M., Virolainen M.,
Konttinen A.;
"Alpha fetoprotein: structure and expression in man and inbred mouse
strains under normal conditions and liver injury.";
Johns Hopkins Med. J. Suppl. 3:249-255(1974).
[13]
METAL-BINDING.
PubMed=80265;
Aoyagi Y., Ikenaka T., Ichida F.;
"Copper(II)-binding ability of human alpha-fetoprotein.";
Cancer Res. 38:3483-3486(1978).
[14]
BILIRUBIN-BINDING.
PubMed=89900;
Aoyagi Y., Ikenaka T., Ichida F.;
"Alpha-fetoprotein as a carrier protein in plasma and its bilirubin-
binding ability.";
Cancer Res. 39:3571-3574(1979).
[15]
SULFATION.
PubMed=2414772; DOI=10.1073/pnas.82.21.7160;
Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.;
"Tyrosine sulfation of proteins from the human hepatoma cell line
HepG2.";
Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985).
[16]
INVOLVEMENT IN AFPD.
PubMed=15280901; DOI=10.1038/sj.ejhg.5201246;
Sharony R., Zadik I., Parvari R.;
"Congenital deficiency of alpha feto-protein.";
Eur. J. Hum. Genet. 12:871-874(2004).
[17]
INVOLVEMENT IN AFPD.
PubMed=18854864; DOI=10.1038/ejhg.2008.186;
Petit F.M., Hebert M., Picone O., Brisset S., Maurin M.L., Parisot F.,
Capel L., Benattar C., Senat M.V., Tachdjian G., Labrune P.;
"A new mutation in the AFP gene responsible for a total absence of
alpha feto-protein on second trimester maternal serum screening for
Down syndrome.";
Eur. J. Hum. Genet. 17:387-390(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION AT SER-111; SER-115; SER-117; SER-344; SER-444 AND
SER-445.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
-!- FUNCTION: Binds copper, nickel, and fatty acids as well as, and
bilirubin less well than, serum albumin. Only a small percentage
(less than 2%) of the human AFP shows estrogen-binding properties.
-!- SUBUNIT: Dimeric and trimeric forms have been found in addition to
the monomeric form.
-!- INTERACTION:
Q99IB8:- (xeno); NbExp=2; IntAct=EBI-722498, EBI-6901449;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma. Synthesized by the fetal liver and
yolk sac.
-!- DEVELOPMENTAL STAGE: Occurs in the plasma of fetuses more than 4
weeks old, reaches the highest levels during the 12th-16th week of
gestation, and drops to trace amounts after birth. The serum level
in adults is usually less than 40 ng/ml. AFP occurs also at high
levels in the plasma and ascitic fluid of adults with hepatoma.
-!- PTM: Independent studies suggest heterogeneity of the N-terminal
sequence of the mature protein and of the cleavage site of the
signal sequence.
-!- PTM: Sulfated. {ECO:0000269|PubMed:2414772}.
-!- DISEASE: Alpha-fetoprotein deficiency (AFPD) [MIM:615969]: A
benign condition characterized by undetectable AFP levels in the
amniotic fluid. Affected individuals are asymptomatic and present
normal development. {ECO:0000269|PubMed:15280901,
ECO:0000269|PubMed:18854864}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Alpha-fetoprotein, hereditary persistence (HPAFP)
[MIM:615970]: A benign autosomal dominant condition characterized
by continued expression of alpha-fetoprotein in adult life.
{ECO:0000269|PubMed:7684942}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
{ECO:0000255|PROSITE-ProRule:PRU00769}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-fetoprotein entry;
URL="https://en.wikipedia.org/wiki/Alpha-fetoprotein";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AFPID44248ch4q13.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; V01514; CAA24758.1; -; mRNA.
EMBL; M16110; AAB58754.1; -; Genomic_DNA.
EMBL; AK314817; BAG37340.1; -; mRNA.
EMBL; BC027881; AAH27881.1; -; mRNA.
EMBL; M10949; AAA51674.1; -; Genomic_DNA.
EMBL; M10950; AAA51675.1; -; Genomic_DNA.
EMBL; Z19532; CAA79592.1; -; Genomic_DNA.
CCDS; CCDS3556.1; -.
PIR; A26624; FPHU.
RefSeq; NP_001125.1; NM_001134.2.
UniGene; Hs.518808; -.
PDB; 3MRK; X-ray; 1.40 A; P=137-145.
PDBsum; 3MRK; -.
ProteinModelPortal; P02771; -.
SMR; P02771; -.
BioGrid; 106682; 11.
IntAct; P02771; 10.
MINT; MINT-1401527; -.
STRING; 9606.ENSP00000379138; -.
iPTMnet; P02771; -.
PhosphoSitePlus; P02771; -.
UniCarbKB; P02771; -.
BioMuta; AFP; -.
DMDM; 120042; -.
MaxQB; P02771; -.
PaxDb; P02771; -.
PeptideAtlas; P02771; -.
PRIDE; P02771; -.
TopDownProteomics; P02771; -.
DNASU; 174; -.
Ensembl; ENST00000395792; ENSP00000379138; ENSG00000081051.
GeneID; 174; -.
KEGG; hsa:174; -.
UCSC; uc003hgz.3; human.
CTD; 174; -.
DisGeNET; 174; -.
GeneCards; AFP; -.
HGNC; HGNC:317; AFP.
HPA; CAB024283; -.
HPA; CAB025339; -.
HPA; HPA010607; -.
HPA; HPA023600; -.
MalaCards; AFP; -.
MIM; 104150; gene.
MIM; 615969; phenotype.
MIM; 615970; phenotype.
neXtProt; NX_P02771; -.
OpenTargets; ENSG00000081051; -.
Orphanet; 168612; Congenital deficiency in alpha-fetoprotein.
Orphanet; 168615; Hereditary persistence of alpha-fetoprotein.
PharmGKB; PA24614; -.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
GeneTree; ENSGT00390000000113; -.
HOGENOM; HOG000293137; -.
HOVERGEN; HBG004207; -.
InParanoid; P02771; -.
KO; K16144; -.
PhylomeDB; P02771; -.
TreeFam; TF335561; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; AFP; human.
GeneWiki; Alpha-fetoprotein; -.
GenomeRNAi; 174; -.
PRO; PR:P02771; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000081051; -.
CleanEx; HS_AFP; -.
ExpressionAtlas; P02771; baseline and differential.
Genevisible; P02771; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0042448; P:progesterone metabolic process; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
GO; GO:0006810; P:transport; IEA:InterPro.
CDD; cd00015; ALBUMIN; 3.
InterPro; IPR000264; ALB/AFP/VDB.
InterPro; IPR020858; Serum_albumin-like.
InterPro; IPR021177; Serum_albumin/AFP/Afamin.
InterPro; IPR020857; Serum_albumin_CS.
InterPro; IPR014760; Serum_albumin_N.
PANTHER; PTHR11385; PTHR11385; 1.
Pfam; PF00273; Serum_albumin; 3.
PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
PRINTS; PR00803; AFETOPROTEIN.
PRINTS; PR00802; SERUMALBUMIN.
SMART; SM00103; ALBUMIN; 3.
SUPFAM; SSF48552; SSF48552; 3.
PROSITE; PS00212; ALBUMIN_1; 2.
PROSITE; PS51438; ALBUMIN_2; 3.
1: Evidence at protein level;
3D-structure; Complete proteome; Copper; Direct protein sequencing;
Disulfide bond; Glycoprotein; Metal-binding; Nickel; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal; Sulfation.
SIGNAL 1 18 {ECO:0000269|PubMed:1709810}.
CHAIN 19 609 Alpha-fetoprotein.
/FTId=PRO_0000001097.
DOMAIN 19 210 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 211 402 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 403 601 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
METAL 22 22 Copper or nickel.
{ECO:0000269|PubMed:80265}.
MOD_RES 111 111 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 115 115 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 117 117 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 344 344 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 444 444 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 445 445 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000070.
DISULFID 99 114
DISULFID 113 124
DISULFID 148 193
DISULFID 192 201
DISULFID 224 270
DISULFID 269 277
DISULFID 289 303
DISULFID 302 313
DISULFID 384 393
DISULFID 416 462
DISULFID 461 472
DISULFID 485 501
DISULFID 500 511
DISULFID 538 583
DISULFID 582 591
VARIANT 187 187 K -> Q (in dbSNP:rs35765619).
/FTId=VAR_033928.
VARIANT 570 570 A -> G (in dbSNP:rs7790).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_012049.
SEQUENCE 609 AA; 68678 MW; 4D4E45820E1C2D4F CRC64;
MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF FAQFVQEATY
KEVSKMVKDA LTAIEKPTGD EQSSGCLENQ LPAFLEELCH EKEILEKYGH SDCCSQSEEG
RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA YEEDRETFMN KFIYEIARRH PFLYAPTILL
WAARYDKIIP SCCKAENAVE CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV
TKLSQKFTKV NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT
ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF LASFVHEYSR
RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE LQKYIQESQA LAKRSCGLFQ
KLGEYYLQNA FLVAYTKKAP QLTSSELMAI TRKMAATAAT CCQLSEDKLL ACGEGAADII
IGHLCIRHEM TPVNPGVGQC CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA
QGVALQTMKQ EFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEV CFAEEGQKLI
SKTRAALGV


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