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P43652 (AFAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Afamin
Alternative name(s):
Alpha-albumin
Short name=Alpha-Alb
Gene names
Name:AFM
Synonyms:ALB2, ALBA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vitamin E binding protein. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the regulation and transport of vitamin E at the blood-brain barrier. Ref.8 Ref.9 Ref.13

Subcellular location

Secreted.

Tissue specificity

High level detected in plasma but also in extravascular fluids such as follicular and cerebrospinal fluids (at protein level). Ref.8

Post-translational modification

N-glycosylated; more than 90% of the glycans are sialylated. Ref.8 Ref.15

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Ontologies

Keywords
   Biological processTransport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processvitamin transport

Inferred from direct assay Ref.13. Source: UniProtKB

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Traceable author statement Ref.1. Source: ProtInc

extracellular space

Inferred from direct assay Ref.8Ref.13. Source: UniProtKB

   Molecular_functionvitamin E binding

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.8
Chain22 – 599578Afamin
PRO_0000001106

Regions

Domain22 – 210189Albumin 1
Domain211 – 403193Albumin 2
Domain404 – 599196Albumin 3

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) (complex) Ref.11 Ref.12 Ref.14 Ref.15
Glycosylation1091N-linked (GlcNAc...) (complex) Ref.16
Glycosylation3831N-linked (GlcNAc...) (complex); atypical Ref.15 Ref.16
Glycosylation4021N-linked (GlcNAc...) (complex) Ref.10 Ref.11 Ref.14 Ref.15 Ref.16
Glycosylation4881N-linked (GlcNAc...) Ref.11
Disulfide bond77 ↔ 86 By similarity
Disulfide bond99 ↔ 114 By similarity
Disulfide bond113 ↔ 124 By similarity
Disulfide bond148 ↔ 193 By similarity
Disulfide bond192 ↔ 201 By similarity
Disulfide bond224 ↔ 270 By similarity
Disulfide bond269 ↔ 277 By similarity
Disulfide bond289 ↔ 303 By similarity
Disulfide bond302 ↔ 313 By similarity
Disulfide bond340 ↔ 385 By similarity
Disulfide bond384 ↔ 393 By similarity
Disulfide bond416 ↔ 462 By similarity
Disulfide bond461 ↔ 470 By similarity
Disulfide bond483 ↔ 499 By similarity
Disulfide bond498 ↔ 509 By similarity
Disulfide bond536 ↔ 581 By similarity
Disulfide bond580 ↔ 589 By similarity

Natural variations

Natural variant3951R → H.
Corresponds to variant rs41265665 [ dbSNP | Ensembl ].
VAR_061003
Natural variant4041T → S.
Corresponds to variant rs2276444 [ dbSNP | Ensembl ].
VAR_048218

Sequences

Sequence LengthMass (Da)Tools
P43652 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D594E75E20D308AB

FASTA59969,069
        10         20         30         40         50         60 
MKLLKLTGFI FFLFFLTESL TLPTQPRDIE NFNSTQKFIE DNIEYITIIA FAQYVQEATF 

        70         80         90        100        110        120 
EEMEKLVKDM VEYKDRCMAD KTLPECSKLP NNVLQEKICA MEGLPQKHNF SHCCSKVDAQ 

       130        140        150        160        170        180 
RRLCFFYNKK SDVGFLPPFP TLDPEEKCQA YESNRESLLN HFLYEVARRN PFVFAPTLLT 

       190        200        210        220        230        240 
VAVHFEEVAK SCCEEQNKVN CLQTRAIPVT QYLKAFSSYQ KHVCGALLKF GTKVVHFIYI 

       250        260        270        280        290        300 
AILSQKFPKI EFKELISLVE DVSSNYDGCC EGDVVQCIRD TSKVMNHICS KQDSISSKIK 

       310        320        330        340        350        360 
ECCEKKIPER GQCIINSNKD DRPKDLSLRE GKFTDSENVC QERDADPDTF FAKFTFEYSR 

       370        380        390        400        410        420 
RHPDLSIPEL LRIVQIYKDL LRNCCNTENP PGCYRYAEDK FNETTEKSLK MVQQECKHFQ 

       430        440        450        460        470        480 
NLGKDGLKYH YLIRLTKIAP QLSTEELVSL GEKMVTAFTT CCTLSEEFAC VDNLADLVFG 

       490        500        510        520        530        540 
ELCGVNENRT INPAVDHCCK TNFAFRRPCF ESLKADKTYV PPPFSQDLFT FHADMCQSQN 

       550        560        570        580        590 
EELQRKTDRF LVNLVKLKHE LTDEELQSLF TNFANVVDKC CKAESPEVCF NEESPKIGN 

« Hide

References

« Hide 'large scale' references
[1]"Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family."
Lichenstein H.S., Lyons D.E., Wurfel M.M., Johnson D.A., McGinley M.D., Leidli J.C., Trollinger D.B., Mayer J.P., Wright S.D., Zukowski M.M.
J. Biol. Chem. 269:18149-18154(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Complete structure of the human alpha-albumin gene, a new member of the serum albumin multigene family."
Nishio H., Dugaiczyk A.
Proc. Natl. Acad. Sci. U.S.A. 93:7557-7561(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
[7]"Identification of rat alpha-albumin and cDNA cloning of its human ortholog."
Allard D., Gilbert S., Lamontagne A., Hamel D., Belanger L.
Gene 153:287-288(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-69; 105-207 AND 560-599.
Tissue: Liver.
[8]"Afamin is a novel human vitamin E-binding glycoprotein characterization and in vitro expression."
Jerkovic L., Voegele A.F., Chwatal S., Kronenberg F., Radcliffe C.M., Wormald M.R., Lobentanz E.M., Ezeh B., Eller P., Dejori N., Dieplinger B., Lottspeich F., Sattler W., Uhr M., Mechtler K., Dwek R.A., Rudd P.M., Baier G., Dieplinger H.
J. Proteome Res. 4:889-899(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-45, GLYCOSYLATION, TISSUE SPECIFICITY, FUNCTION.
[9]"Characterization of the vitamin E-binding properties of human plasma afamin."
Voegele A.F., Jerkovic L., Wellenzohn B., Eller P., Kronenberg F., Liedl K.R., Dieplinger H.
Biochemistry 41:14532-14538(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-402.
Tissue: Plasma.
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-402 AND ASN-488.
Tissue: Plasma.
[12]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33.
Tissue: Saliva.
[13]"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: FUNCTION.
[14]"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.
[15]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-33; ASN-383 AND ASN-402.
[16]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-383 AND ASN-402, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L32140 mRNA. Translation: AAA21612.1.
U51243 Genomic DNA. Translation: AAC50720.1.
AK290556 mRNA. Translation: BAF83245.1.
AC108157 Genomic DNA. No translation available.
AC110752 Genomic DNA. Translation: AAY41051.1.
CH471057 Genomic DNA. Translation: EAX05682.1.
BC109020 mRNA. Translation: AAI09021.1.
BC109021 mRNA. Translation: AAI09022.1.
L35486 mRNA. Translation: AAA68197.1.
L35497 mRNA. Translation: AAA68198.1.
L35498 mRNA. Translation: AAA68199.1.
PIRA54906.
I39424.
I39426.
RefSeqNP_001124.1. NM_001133.2.
UniGeneHs.168718.

3D structure databases

ProteinModelPortalP43652.
SMRP43652. Positions 40-597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000226355.

PTM databases

PhosphoSiteP43652.

Polymorphism databases

DMDM1168366.

Proteomic databases

PaxDbP43652.
PeptideAtlasP43652.
PRIDEP43652.

Protocols and materials databases

DNASU173.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226355; ENSP00000226355; ENSG00000079557.
GeneID173.
KEGGhsa:173.
UCSCuc003hhb.3. human.

Organism-specific databases

CTD173.
GeneCardsGC04P074336.
HGNCHGNC:316. AFM.
HPAHPA017006.
MIM104145. gene.
neXtProtNX_P43652.
PharmGKBPA24613.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47806.
HOGENOMHOG000293137.
HOVERGENHBG004207.
InParanoidP43652.
OMAFACVDNL.
OrthoDBEOG7DZ8JF.
PhylomeDBP43652.
TreeFamTF335561.

Gene expression databases

BgeeP43652.
CleanExHS_AFM.
GenevestigatorP43652.

Family and domain databases

InterProIPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMSSF48552. SSF48552. 3 hits.
PROSITEPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAFM. human.
GeneWikiAfamin.
GenomeRNAi173.
NextBio694.
PROP43652.
SOURCESearch...

Entry information

Entry nameAFAM_HUMAN
AccessionPrimary (citable) accession number: P43652
Secondary accession number(s): A8K3E1, Q32MR3, Q4W5C5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM