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Protein

Alpha-fetoprotein

Gene

Afp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Binds estrogens, fatty acids and metals.

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. ovulation from ovarian follicle Source: MGI
  2. progesterone metabolic process Source: MGI
  3. sexual reproduction Source: MGI
  4. SMAD protein signal transduction Source: MGI
  5. transport Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Copper, Metal-binding, Nickel

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-fetoprotein
Alternative name(s):
Alpha-1-fetoprotein
Alpha-fetoglobulin
Gene namesi
Name:Afp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:87951. Afp.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 605587Alpha-fetoproteinPRO_0000001098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi95 ↔ 110PROSITE-ProRule annotation
Disulfide bondi109 ↔ 120PROSITE-ProRule annotation
Disulfide bondi144 ↔ 189PROSITE-ProRule annotation
Disulfide bondi188 ↔ 197PROSITE-ProRule annotation
Disulfide bondi220 ↔ 266PROSITE-ProRule annotation
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi265 ↔ 273PROSITE-ProRule annotation
Disulfide bondi285 ↔ 299PROSITE-ProRule annotation
Disulfide bondi298 ↔ 309PROSITE-ProRule annotation
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi380 ↔ 389PROSITE-ProRule annotation
Disulfide bondi412 ↔ 458PROSITE-ProRule annotation
Disulfide bondi457 ↔ 468PROSITE-ProRule annotation
Disulfide bondi481 ↔ 497PROSITE-ProRule annotation
Disulfide bondi496 ↔ 507PROSITE-ProRule annotation
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi534 ↔ 579PROSITE-ProRule annotation
Disulfide bondi578 ↔ 587PROSITE-ProRule annotation

Post-translational modificationi

Glycosylated; contains two glycans.
Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

MaxQBiP02772.
PaxDbiP02772.
PRIDEiP02772.

2D gel databases

REPRODUCTION-2DPAGEIPI00113163.

PTM databases

PhosphoSiteiP02772.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP02772.
CleanExiMM_AFP.
ExpressionAtlasiP02772. baseline and differential.
GenevestigatoriP02772.

Structurei

3D structure databases

ProteinModelPortaliP02772.
SMRiP02772. Positions 40-604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 207189Albumin 1PROSITE-ProRule annotationAdd
BLAST
Domaini208 – 398191Albumin 2PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 597199Albumin 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
Contains 3 albumin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG45992.
GeneTreeiENSGT00390000000113.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02772.
KOiK16144.
OMAiFHKDLCQ.
OrthoDBiEOG7S4X5C.
PhylomeDBiP02772.
TreeFamiTF335561.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 2 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02772-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKWITPASLI LLLHFAASKA LHENEFGIAS TLDSSQCVTE KNVLSIATIT
60 70 80 90 100
FTQFVPEATE EEVNKMTSDV LAAMKKNSGD GCLESQLSVF LDEICHETEL
110 120 130 140 150
SNKYGLSGCC SQSGVERHQC LLARKKTAPA SVPPFQFPEP AESCKAHEEN
160 170 180 190 200
RAVFMNRFIY EVSRRNPFMY APAILSLAAQ YDKVVLACCK ADNKEECFQT
210 220 230 240 250
KRASIAKELR EGSMLNEHVC SVIRKFGSRN LQATTIIKLS QKLTEANFTE
260 270 280 290 300
IQKLALDVAH IHEECCQGNS LECLQDGEKV MTYICSQQNI LSSKIAECCK
310 320 330 340 350
LPMIQLGFCI IHAENGVKPE GLSLNPSQFL GDRNFAQFSS EEKIMFMASF
360 370 380 390 400
LHEYSRTHPN LPVSVILRIA KTYQEILEKC SQSGNLPGCQ DNLEEELQKH
410 420 430 440 450
IEESQALSKQ SCALYQTLGD YKLQNLFLIG YTRKAPQLTS AELIDLTGKM
460 470 480 490 500
VSIASTCCQL SEEKWSGCGE GMADIFIGHL CIRNEASPVN SGISHCCNSS
510 520 530 540 550
YSNRRLCITS FLRDETYAPP PFSEDKFIFH KDLCQAQGKA LQTMKQELLI
560 570 580 590 600
NLVKQKPELT EEQLAAVTAD FSGLLEKCCK AQDQEVCFTE EGPKLISKTR

DALGV
Length:605
Mass (Da):67,337
Last modified:July 21, 1986 - v1
Checksum:iCE09E9F50D74619A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti533 – 5364LCQA → RAKL no nucleotide entry (PubMed:6161929)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00743 mRNA. Translation: CAA24118.1.
M16394
, M16381, M16382, M16383, M16384, M16385, M16386, M16387, M16388, M16389, M16390, M16391, M16392, M16393 Genomic DNA. Translation: AAA37189.1.
AK010934 mRNA. Translation: BAB27278.1.
AK145975 mRNA. Translation: BAE26798.1.
AK146513 mRNA. Translation: BAE27225.1.
AK146524 mRNA. Translation: BAE27233.1.
AK167549 mRNA. Translation: BAE39615.1.
AK168574 mRNA. Translation: BAE40444.1.
AK168576 mRNA. Translation: BAE40446.1.
AK168751 mRNA. Translation: BAE40591.1.
AK168883 mRNA. Translation: BAE40701.1.
AK169046 mRNA. Translation: BAE40834.1.
AK169054 mRNA. Translation: BAE40842.1.
AK169147 mRNA. Translation: BAE40926.1.
BC066206 mRNA. Translation: AAH66206.1.
CCDSiCCDS19413.1.
PIRiA93254. FPMS.
RefSeqiNP_031449.3. NM_007423.4.
UniGeneiMm.358570.

Genome annotation databases

EnsembliENSMUST00000042755; ENSMUSP00000041006; ENSMUSG00000054932.
GeneIDi11576.
KEGGimmu:11576.
UCSCiuc008yba.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00743 mRNA. Translation: CAA24118.1.
M16394
, M16381, M16382, M16383, M16384, M16385, M16386, M16387, M16388, M16389, M16390, M16391, M16392, M16393 Genomic DNA. Translation: AAA37189.1.
AK010934 mRNA. Translation: BAB27278.1.
AK145975 mRNA. Translation: BAE26798.1.
AK146513 mRNA. Translation: BAE27225.1.
AK146524 mRNA. Translation: BAE27233.1.
AK167549 mRNA. Translation: BAE39615.1.
AK168574 mRNA. Translation: BAE40444.1.
AK168576 mRNA. Translation: BAE40446.1.
AK168751 mRNA. Translation: BAE40591.1.
AK168883 mRNA. Translation: BAE40701.1.
AK169046 mRNA. Translation: BAE40834.1.
AK169054 mRNA. Translation: BAE40842.1.
AK169147 mRNA. Translation: BAE40926.1.
BC066206 mRNA. Translation: AAH66206.1.
CCDSiCCDS19413.1.
PIRiA93254. FPMS.
RefSeqiNP_031449.3. NM_007423.4.
UniGeneiMm.358570.

3D structure databases

ProteinModelPortaliP02772.
SMRiP02772. Positions 40-604.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiP02772.

2D gel databases

REPRODUCTION-2DPAGEIPI00113163.

Proteomic databases

MaxQBiP02772.
PaxDbiP02772.
PRIDEiP02772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042755; ENSMUSP00000041006; ENSMUSG00000054932.
GeneIDi11576.
KEGGimmu:11576.
UCSCiuc008yba.2. mouse.

Organism-specific databases

CTDi174.
MGIiMGI:87951. Afp.

Phylogenomic databases

eggNOGiNOG45992.
GeneTreeiENSGT00390000000113.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02772.
KOiK16144.
OMAiFHKDLCQ.
OrthoDBiEOG7S4X5C.
PhylomeDBiP02772.
TreeFamiTF335561.

Miscellaneous databases

ChiTaRSiAfp. mouse.
NextBioi279098.
PROiP02772.
SOURCEiSearch...

Gene expression databases

BgeeiP02772.
CleanExiMM_AFP.
ExpressionAtlasiP02772. baseline and differential.
GenevestigatoriP02772.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 2 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Homology between the primary structure of alpha-fetoprotein, deduced from a complete cDNA sequence, and serum albumin."
    Law S.W., Dugaiczyk A.
    Nature 291:201-205(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The rate of molecular evolution of alpha-fetoprotein approaches that of pseudogenes."
    Minghetti P.P., Law S.W., Dugaiczyk A.
    Mol. Biol. Evol. 2:347-358(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 598.
  3. "Intragenic amplification and divergence in the mouse alpha-fetoprotein gene."
    Eiferman F.A., Young P.R., Scott R.W., Tilghman S.M.
    Nature 294:713-718(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Liver and Placenta.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  6. "The evolution of alpha-fetoprotein and albumin. I. A comparison of the primary amino acid sequences of mammalian alpha-fetoprotein and albumin."
    Gorin M.B., Cooper D.L., Eiferman F.A., van de Rijn P., Tilghman S.M.
    J. Biol. Chem. 256:1954-1959(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-605.

Entry informationi

Entry nameiFETA_MOUSE
AccessioniPrimary (citable) accession number: P02772
Secondary accession number(s): Q3UJD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.