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P43652

- AFAM_HUMAN

UniProt

P43652 - AFAM_HUMAN

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Protein
Afamin
Gene
AFM, ALB2, ALBA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. vitamin E binding Source: UniProtKB

GO - Biological processi

  1. vitamin transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Afamin
Alternative name(s):
Alpha-albumin
Short name:
Alpha-Alb
Gene namesi
Name:AFM
Synonyms:ALB2, ALBA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:316. AFM.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: ProtInc
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24613.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 Publication
Add
BLAST
Chaini22 – 599578Afamin
PRO_0000001106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...) (complex)4 Publications
Disulfide bondi77 ↔ 86 By similarity
Disulfide bondi99 ↔ 114 By similarity
Glycosylationi109 – 1091N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi113 ↔ 124 By similarity
Disulfide bondi148 ↔ 193 By similarity
Disulfide bondi192 ↔ 201 By similarity
Disulfide bondi224 ↔ 270 By similarity
Disulfide bondi269 ↔ 277 By similarity
Disulfide bondi289 ↔ 303 By similarity
Disulfide bondi302 ↔ 313 By similarity
Disulfide bondi340 ↔ 385 By similarity
Glycosylationi383 – 3831N-linked (GlcNAc...) (complex); atypical2 Publications
Disulfide bondi384 ↔ 393 By similarity
Glycosylationi402 – 4021N-linked (GlcNAc...) (complex)5 Publications
Disulfide bondi416 ↔ 462 By similarity
Disulfide bondi461 ↔ 470 By similarity
Disulfide bondi483 ↔ 499 By similarity
Glycosylationi488 – 4881N-linked (GlcNAc...)1 Publication
Disulfide bondi498 ↔ 509 By similarity
Disulfide bondi536 ↔ 581 By similarity
Disulfide bondi580 ↔ 589 By similarity

Post-translational modificationi

N-glycosylated; more than 90% of the glycans are sialylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP43652.
PeptideAtlasiP43652.
PRIDEiP43652.

PTM databases

PhosphoSiteiP43652.

Expressioni

Tissue specificityi

High level detected in plasma but also in extravascular fluids such as follicular and cerebrospinal fluids (at protein level).1 Publication

Gene expression databases

BgeeiP43652.
CleanExiHS_AFM.
GenevestigatoriP43652.

Organism-specific databases

HPAiHPA017006.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000226355.

Structurei

3D structure databases

ProteinModelPortaliP43652.
SMRiP43652. Positions 40-597.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 210189Albumin 1
Add
BLAST
Domaini211 – 403193Albumin 2
Add
BLAST
Domaini404 – 599196Albumin 3
Add
BLAST

Sequence similaritiesi

Belongs to the ALB/AFP/VDB family.
Contains 3 albumin domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG47806.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP43652.
OMAiFACVDNL.
OrthoDBiEOG7DZ8JF.
PhylomeDBiP43652.
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. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43652-1 [UniParc]FASTAAdd to Basket

« Hide

MKLLKLTGFI FFLFFLTESL TLPTQPRDIE NFNSTQKFIE DNIEYITIIA    50
FAQYVQEATF EEMEKLVKDM VEYKDRCMAD KTLPECSKLP NNVLQEKICA 100
MEGLPQKHNF SHCCSKVDAQ RRLCFFYNKK SDVGFLPPFP TLDPEEKCQA 150
YESNRESLLN HFLYEVARRN PFVFAPTLLT VAVHFEEVAK SCCEEQNKVN 200
CLQTRAIPVT QYLKAFSSYQ KHVCGALLKF GTKVVHFIYI AILSQKFPKI 250
EFKELISLVE DVSSNYDGCC EGDVVQCIRD TSKVMNHICS KQDSISSKIK 300
ECCEKKIPER GQCIINSNKD DRPKDLSLRE GKFTDSENVC QERDADPDTF 350
FAKFTFEYSR RHPDLSIPEL LRIVQIYKDL LRNCCNTENP PGCYRYAEDK 400
FNETTEKSLK MVQQECKHFQ NLGKDGLKYH YLIRLTKIAP QLSTEELVSL 450
GEKMVTAFTT CCTLSEEFAC VDNLADLVFG ELCGVNENRT INPAVDHCCK 500
TNFAFRRPCF ESLKADKTYV PPPFSQDLFT FHADMCQSQN EELQRKTDRF 550
LVNLVKLKHE LTDEELQSLF TNFANVVDKC CKAESPEVCF NEESPKIGN 599
Length:599
Mass (Da):69,069
Last modified:November 1, 1995 - v1
Checksum:iD594E75E20D308AB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti395 – 3951R → H.
Corresponds to variant rs41265665 [ dbSNP | Ensembl ].
VAR_061003
Natural varianti404 – 4041T → S.
Corresponds to variant rs2276444 [ dbSNP | Ensembl ].
VAR_048218

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3557.1.
PIRiA54906.
I39424.
I39426.
RefSeqiNP_001124.1. NM_001133.2.
UniGeneiHs.168718.

Genome annotation databases

EnsembliENST00000226355; ENSP00000226355; ENSG00000079557.
GeneIDi173.
KEGGihsa:173.
UCSCiuc003hhb.3. human.

Polymorphism databases

DMDMi1168366.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3557.1.
PIRi A54906.
I39424.
I39426.
RefSeqi NP_001124.1. NM_001133.2.
UniGenei Hs.168718.

3D structure databases

ProteinModelPortali P43652.
SMRi P43652. Positions 40-597.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000226355.

PTM databases

PhosphoSitei P43652.

Polymorphism databases

DMDMi 1168366.

Proteomic databases

PaxDbi P43652.
PeptideAtlasi P43652.
PRIDEi P43652.

Protocols and materials databases

DNASUi 173.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000226355 ; ENSP00000226355 ; ENSG00000079557 .
GeneIDi 173.
KEGGi hsa:173.
UCSCi uc003hhb.3. human.

Organism-specific databases

CTDi 173.
GeneCardsi GC04P074336.
HGNCi HGNC:316. AFM.
HPAi HPA017006.
MIMi 104145. gene.
neXtProti NX_P43652.
PharmGKBi PA24613.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47806.
HOGENOMi HOG000293137.
HOVERGENi HBG004207.
InParanoidi P43652.
OMAi FACVDNL.
OrthoDBi EOG7DZ8JF.
PhylomeDBi P43652.
TreeFami TF335561.

Miscellaneous databases

ChiTaRSi AFM. human.
GeneWikii Afamin.
GenomeRNAii 173.
NextBioi 694.
PROi P43652.
SOURCEi Search...

Gene expression databases

Bgeei P43652.
CleanExi HS_AFM.
Genevestigatori P43652.

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. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAFAM_HUMAN
AccessioniPrimary (citable) accession number: P43652
Secondary accession number(s): A8K3E1, Q32MR3, Q4W5C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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