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O89020

- AFAM_MOUSE

UniProt

O89020 - AFAM_MOUSE

Protein

Afamin

Gene

Afm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Vitamin E binding protein. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient or across the blood-brain barrier By similarity.By similarity

    GO - Molecular functioni

    1. vitamin E binding Source: UniProtKB

    GO - Biological processi

    1. vitamin transport Source: UniProtKB

    Keywords - Biological processi

    Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Afamin
    Alternative name(s):
    Alpha-albumin
    Short name:
    Alpha-Alb
    Gene namesi
    Name:Afm
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2429409. Afm.

    Subcellular locationi

    Secreted
    Note: Detected in large and small blood vessels throughout the cortex and the striatum.

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121By similarityAdd
    BLAST
    Chaini22 – 608587AfaminPRO_0000001107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331N-linked (GlcNAc...)3 Publications
    Disulfide bondi77 ↔ 86PROSITE-ProRule annotation
    Disulfide bondi99 ↔ 114PROSITE-ProRule annotation
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi113 ↔ 124PROSITE-ProRule annotation
    Disulfide bondi148 ↔ 193PROSITE-ProRule annotation
    Glycosylationi153 – 1531N-linked (GlcNAc...)1 Publication
    Disulfide bondi224 ↔ 270PROSITE-ProRule annotation
    Disulfide bondi269 ↔ 277PROSITE-ProRule annotation
    Disulfide bondi289 ↔ 303PROSITE-ProRule annotation
    Disulfide bondi302 ↔ 313PROSITE-ProRule annotation
    Disulfide bondi340 ↔ 385PROSITE-ProRule annotation
    Disulfide bondi384 ↔ 393PROSITE-ProRule annotation
    Glycosylationi402 – 4021N-linked (GlcNAc...)3 Publications
    Disulfide bondi416 ↔ 462PROSITE-ProRule annotation
    Disulfide bondi461 ↔ 470PROSITE-ProRule annotation
    Disulfide bondi483 ↔ 499PROSITE-ProRule annotation
    Glycosylationi488 – 4881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi498 ↔ 509PROSITE-ProRule annotation
    Disulfide bondi580 ↔ 589PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated; more than 90% of the glycans are sialylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO89020.
    PaxDbiO89020.
    PRIDEiO89020.

    PTM databases

    PhosphoSiteiO89020.

    Expressioni

    Tissue specificityi

    Detected in brain (at protein level). Expressed in isolated brain capillaries.1 Publication

    Gene expression databases

    BgeeiO89020.
    CleanExiMM_AFM.
    GenevestigatoriO89020.

    Interactioni

    Protein-protein interaction databases

    IntActiO89020. 1 interaction.
    MINTiMINT-4087327.

    Structurei

    3D structure databases

    ProteinModelPortaliO89020.
    SMRiO89020. Positions 40-603.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 210189Albumin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini211 – 403193Albumin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini404 – 599196Albumin 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

    eggNOGiNOG47806.
    GeneTreeiENSGT00390000000113.
    HOGENOMiHOG000293137.
    HOVERGENiHBG004207.
    InParanoidiO89020.
    OMAiFACVDNL.
    OrthoDBiEOG7DZ8JF.
    PhylomeDBiO89020.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O89020-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRHLKLTGFI FFLLPLTESL ALPTKPQDVD HFNATQKFID ENTTYLAIIA    50
    FSQYVQEASF DEVETLVKVM LDYRDRCWAD NTLPECSKTA NDAIQDMLCD 100
    MEGLPQKHNF SHCCGKAGFP RRLCFFYNKK ANVGFLPPFP TLDPEEKCQA 150
    YKNNSESFLH LYMYEVARRN PFVFAPVLLA VAAWFEEAAT TCCEQQQKAT 200
    CFQAKAAPIT QYLKASSSYQ RNVCGALIKF GPKVLNSINV AVFSKKFPKI 250
    GFKDLTTLLE DVSSMYEGCC EGDVVHCIRS QSQVVNHICS KQDSISSKIK 300
    VCCEKKTLER EACIINANKD DRPEGLSLRE AKFTESENVC QERDSDPDKF 350
    FAEFIYEYSR RHPDLSTPEL LRITKVYMDF LEDCCSRENP AGCYRHVEDK 400
    FNETTQRSLA MVQQECKQFQ ELGKDTLQRH FLVKFTKAAP QLPMEELVSL 450
    SKEMVAALTT CCTLSDEFAC VDNLADLVLG ELCGVNTNRT INPAVDHCCK 500
    TDFAFRRHCF EHLKADTTYE LPSVSALVSA LHTDWCQPRK EDLQNKKHRF 550
    LVNLVKWMPG ITDEEWLCLF TKFTAAREEC SEVQEPESCF SPESSKTGDE 600
    SQATEKQR 608
    Length:608
    Mass (Da):69,379
    Last modified:February 20, 2007 - v2
    Checksum:i98B31E6D96E73F12
    GO
    Isoform 2 (identifier: O89020-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         430-430: H → Q
         431-608: Missing.

    Show »
    Length:430
    Mass (Da):49,275
    Checksum:i1CF6CB19386A4976
    GO
    Isoform 3 (identifier: O89020-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         606-608: KQR → NKITDQ

    Note: No experimental confirmation available.

    Show »
    Length:611
    Mass (Da):69,666
    Checksum:iF0EE392CF6F91D96
    GO

    Sequence cautioni

    The sequence AAH26681.1 differs from that shown. Reason: Contaminating sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441T → A in CAA09471. 1 PublicationCurated
    Sequence conflicti44 – 441T → A in AAH26681. (PubMed:15489334)Curated
    Sequence conflicti154 – 1541N → K in CAA09471. 1 PublicationCurated
    Sequence conflicti280 – 2801S → N in AAI00598. (PubMed:15489334)Curated
    Sequence conflicti285 – 2851V → E in CAA09471. 1 PublicationCurated
    Sequence conflicti295 – 2951I → V in AAI00598. (PubMed:15489334)Curated
    Sequence conflicti307 – 3071T → I in AAI00598. (PubMed:15489334)Curated
    Sequence conflicti369 – 3691E → R in CAA09471. 1 PublicationCurated
    Sequence conflicti417 – 4171K → N in CAA09471. 1 PublicationCurated
    Sequence conflicti520 – 5201E → A in CAA09471. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei430 – 4301H → Q in isoform 2. 2 PublicationsVSP_023387
    Alternative sequencei431 – 608178Missing in isoform 2. 2 PublicationsVSP_023388Add
    BLAST
    Alternative sequencei606 – 6083KQR → NKITDQ in isoform 3. 1 PublicationVSP_023389

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011080 mRNA. Translation: CAA09471.1.
    AK143987 mRNA. Translation: BAE25647.1.
    BC026681 mRNA. Translation: AAH26681.1. Sequence problems.
    BC100597 mRNA. Translation: AAI00598.1.
    CCDSiCCDS39141.1. [O89020-1]
    RefSeqiNP_660128.2. NM_145146.2. [O89020-1]
    UniGeneiMm.348786.

    Genome annotation databases

    EnsembliENSMUST00000113179; ENSMUSP00000108804; ENSMUSG00000029369. [O89020-1]
    ENSMUST00000128740; ENSMUSP00000117180; ENSMUSG00000029369. [O89020-2]
    GeneIDi280662.
    KEGGimmu:280662.
    UCSCiuc008ybb.1. mouse. [O89020-2]
    uc008ybc.1. mouse. [O89020-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011080 mRNA. Translation: CAA09471.1 .
    AK143987 mRNA. Translation: BAE25647.1 .
    BC026681 mRNA. Translation: AAH26681.1 . Sequence problems.
    BC100597 mRNA. Translation: AAI00598.1 .
    CCDSi CCDS39141.1. [O89020-1 ]
    RefSeqi NP_660128.2. NM_145146.2. [O89020-1 ]
    UniGenei Mm.348786.

    3D structure databases

    ProteinModelPortali O89020.
    SMRi O89020. Positions 40-603.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O89020. 1 interaction.
    MINTi MINT-4087327.

    PTM databases

    PhosphoSitei O89020.

    Proteomic databases

    MaxQBi O89020.
    PaxDbi O89020.
    PRIDEi O89020.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000113179 ; ENSMUSP00000108804 ; ENSMUSG00000029369 . [O89020-1 ]
    ENSMUST00000128740 ; ENSMUSP00000117180 ; ENSMUSG00000029369 . [O89020-2 ]
    GeneIDi 280662.
    KEGGi mmu:280662.
    UCSCi uc008ybb.1. mouse. [O89020-2 ]
    uc008ybc.1. mouse. [O89020-1 ]

    Organism-specific databases

    CTDi 173.
    MGIi MGI:2429409. Afm.

    Phylogenomic databases

    eggNOGi NOG47806.
    GeneTreei ENSGT00390000000113.
    HOGENOMi HOG000293137.
    HOVERGENi HBG004207.
    InParanoidi O89020.
    OMAi FACVDNL.
    OrthoDBi EOG7DZ8JF.
    PhylomeDBi O89020.
    TreeFami TF335561.

    Miscellaneous databases

    ChiTaRSi AFM. mouse.
    NextBioi 394069.
    PROi O89020.
    SOURCEi Search...

    Gene expression databases

    Bgeei O89020.
    CleanExi MM_AFM.
    Genevestigatori O89020.

    Family and domain databases

    InterProi IPR000264. ALB/AFP/VDB.
    IPR001703. Alpha-fetoprotein.
    IPR020858. Serum_albumin-like.
    IPR021177. Serum_albumin/AFP.
    IPR020857. Serum_albumin_CS.
    IPR014760. Serum_albumin_N.
    [Graphical view ]
    Pfami PF00273. Serum_albumin. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF002520. Serum_albumin_subgroup. 1 hit.
    PRINTSi PR00803. AFETOPROTEIN.
    PR00802. SERUMALBUMIN.
    SMARTi SM00103. ALBUMIN. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48552. SSF48552. 3 hits.
    PROSITEi PS00212. ALBUMIN_1. 2 hits.
    PS51438. ALBUMIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. van Reeth T., Gabant P., Dreze P., Szpirer J., Szpirer C.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Diaphragm.
    2. "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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Kidney.
    3. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-608 (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Kidney and Liver.
    4. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-402.
      Strain: C57BL/6.
      Tissue: Plasma.
    5. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
      Bernhard O.K., Kapp E.A., Simpson R.J.
      J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-153 AND ASN-402.
      Strain: C57BL/6.
      Tissue: Plasma.
    6. "Afamin is synthesized by cerebrovascular endothelial cells and mediates alpha-tocopherol transport across an in vitro model of the blood-brain barrier."
      Kratzer I., Bernhart E., Wintersperger A., Hammer A., Waltl S., Malle E., Sperk G., Wietzorrek G., Dieplinger H., Sattler W.
      J. Neurochem. 108:707-718(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-402.
      Tissue: Liver.

    Entry informationi

    Entry nameiAFAM_MOUSE
    AccessioniPrimary (citable) accession number: O89020
    Secondary accession number(s): Q3UNV0, Q497E6, Q8R0J9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 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