AFAM_HUMAN
ID AFAM_HUMAN Reviewed; 599 AA.
AC P43652; A8K3E1; Q32MR3; Q4W5C5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Afamin;
DE AltName: Full=Alpha-albumin {ECO:0000303|PubMed:8755513};
DE Short=Alpha-Alb;
DE Flags: Precursor;
GN Name=AFM; Synonyms=ALB2, ALBA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-56, PARTIAL PROTEIN
RP SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7517938; DOI=10.1016/s0021-9258(17)32429-8;
RA Lichenstein H.S., Lyons D.E., Wurfel M.M., Johnson D.A., McGinley M.D.,
RA Leidli J.C., Trollinger D.B., Mayer J.P., Wright S.D., Zukowski M.M.;
RT "Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-
RT binding protein gene family.";
RL J. Biol. Chem. 269:18149-18154(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8755513; DOI=10.1073/pnas.93.15.7557;
RA Nishio H., Dugaiczyk A.;
RT "Complete structure of the human alpha-albumin gene, a new member of the
RT serum albumin multigene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7557-7561(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-69; 105-207 AND 560-599.
RC TISSUE=Liver;
RX PubMed=7875606; DOI=10.1016/0378-1119(94)00745-e;
RA Allard D., Gilbert S., Lamontagne A., Hamel D., Belanger L.;
RT "Identification of rat alpha-albumin and cDNA cloning of its human
RT ortholog.";
RL Gene 153:287-288(1995).
RN [8]
RP PROTEIN SEQUENCE OF 22-45, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=15952736; DOI=10.1021/pr0500105;
RA Jerkovic L., Voegele A.F., Chwatal S., Kronenberg F., Radcliffe C.M.,
RA Wormald M.R., Lobentanz E.M., Ezeh B., Eller P., Dejori N., Dieplinger B.,
RA Lottspeich F., Sattler W., Uhr M., Mechtler K., Dwek R.A., Rudd P.M.,
RA Baier G., Dieplinger H.;
RT "Afamin is a novel human vitamin E-binding glycoprotein characterization
RT and in vitro expression.";
RL J. Proteome Res. 4:889-899(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12463752; DOI=10.1021/bi026513v;
RA Voegele A.F., Jerkovic L., Wellenzohn B., Eller P., Kronenberg F.,
RA Liedl K.R., Dieplinger H.;
RT "Characterization of the vitamin E-binding properties of human plasma
RT afamin.";
RL Biochemistry 41:14532-14538(2002).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-402.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-402 AND ASN-488.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [13]
RP FUNCTION.
RX PubMed=19046407; DOI=10.1111/j.1471-4159.2008.05796.x;
RA Kratzer I., Bernhart E., Wintersperger A., Hammer A., Waltl S., Malle E.,
RA Sperk G., Wietzorrek G., Dieplinger H., Sattler W.;
RT "Afamin is synthesized by cerebrovascular endothelial cells and mediates
RT alpha-tocopherol transport across an in vitro model of the blood-brain
RT barrier.";
RL J. Neurochem. 108:707-718(2009).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-402.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP GLYCOSYLATION AT ASN-33; ASN-383 AND ASN-402.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-383 AND ASN-402, AND
RP STRUCTURE OF CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=26902720; DOI=10.7554/elife.11621;
RA Mihara E., Hirai H., Yamamoto H., Tamura-Kawakami K., Matano M.,
RA Kikuchi A., Sato T., Takagi J.;
RT "Active and water-soluble form of lipidated Wnt protein is maintained by a
RT serum glycoprotein afamin/alpha-albumin.";
RL Elife 5:0-0(2016).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 22-599 IN COMPLEX WITH
RP PALMITOLEIC ACID, GLYCOSYLATION AT ASN-402 AND ASN-488, DISULFIDE BONDS,
RP AND DOMAIN.
RX PubMed=29153507; DOI=10.1016/j.str.2017.10.006;
RA Naschberger A., Orry A., Lechner S., Bowler M.W., Nurizzo D., Novokmet M.,
RA Keller M.A., Oemer G., Seppi D., Haslbeck M., Pansi K., Dieplinger H.,
RA Rupp B.;
RT "Structural Evidence for a Role of the Multi-functional Human Glycoprotein
RT Afamin in Wnt Transport.";
RL Structure 25:1907-1915(2017).
CC -!- FUNCTION: Functions as carrier for hydrophobic molecules in body fluids
CC (Probable). Essential for the solubility and activity of lipidated Wnt
CC family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A,
CC WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (PubMed:26902720). Binds
CC vitamin E (PubMed:15952736, PubMed:12463752). May transport vitamin E
CC in body fluids under conditions where the lipoprotein system is not
CC sufficient (PubMed:15952736). May be involved in the transport of
CC vitamin E across the blood-brain barrier (PubMed:19046407).
CC {ECO:0000269|PubMed:12463752, ECO:0000269|PubMed:15952736,
CC ECO:0000269|PubMed:19046407, ECO:0000269|PubMed:26902720, ECO:0000305}.
CC -!- SUBUNIT: Forms a 1:1 complex with Wnt family members; interacts with
CC WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B,
CC WNT10A and WNT10B. {ECO:0000269|PubMed:26902720}.
CC -!- INTERACTION:
CC P43652; P56703: WNT3; NbExp=3; IntAct=EBI-20737924, EBI-3644922;
CC P43652; P27467: Wnt3a; Xeno; NbExp=3; IntAct=EBI-20737924, EBI-2899665;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12463752,
CC ECO:0000269|PubMed:15952736, ECO:0000269|PubMed:26902720,
CC ECO:0000269|PubMed:7517938}.
CC -!- TISSUE SPECIFICITY: High level detected in plasma but also in
CC extravascular fluids such as follicular and cerebrospinal fluids (at
CC protein level). {ECO:0000269|PubMed:12463752,
CC ECO:0000269|PubMed:15952736, ECO:0000269|PubMed:7517938}.
CC -!- DOMAIN: The second albumin domain forms a deep binding pocket that
CC contains palmitoleic acid (in vitro) (PubMed:29153507). Palmitoleic
CC acid is most likely not the physiological ligand. Instead, this pocket
CC may accomodate the covalently bound lipid moiety of Wnt family members
CC (Probable). {ECO:0000269|PubMed:29153507, ECO:0000305}.
CC -!- PTM: N-glycosylated; more than 90% of the glycans are sialylated.
CC {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15952736,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:29153507}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; L32140; AAA21612.1; -; mRNA.
DR EMBL; U51243; AAC50720.1; -; Genomic_DNA.
DR EMBL; AK290556; BAF83245.1; -; mRNA.
DR EMBL; AC108157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110752; AAY41051.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05682.1; -; Genomic_DNA.
DR EMBL; BC109020; AAI09021.1; -; mRNA.
DR EMBL; BC109021; AAI09022.1; -; mRNA.
DR EMBL; L35486; AAA68197.1; -; mRNA.
DR EMBL; L35497; AAA68198.1; -; mRNA.
DR EMBL; L35498; AAA68199.1; -; mRNA.
DR CCDS; CCDS3557.1; -.
DR PIR; A54906; A54906.
DR PIR; I39424; I39424.
DR PIR; I39426; I39426.
DR RefSeq; NP_001124.1; NM_001133.2.
DR PDB; 5OKL; X-ray; 2.09 A; A/B=22-599.
DR PDB; 6FAK; X-ray; 1.90 A; A=22-599.
DR PDB; 6RQ7; X-ray; 2.69 A; B=22-599.
DR PDBsum; 5OKL; -.
DR PDBsum; 6FAK; -.
DR PDBsum; 6RQ7; -.
DR AlphaFoldDB; P43652; -.
DR SMR; P43652; -.
DR BioGRID; 106681; 11.
DR IntAct; P43652; 21.
DR STRING; 9606.ENSP00000226355; -.
DR DrugBank; DB09130; Copper.
DR GlyConnect; 731; 21 N-Linked glycans (6 sites).
DR GlyGen; P43652; 6 sites, 29 N-linked glycans (6 sites).
DR iPTMnet; P43652; -.
DR PhosphoSitePlus; P43652; -.
DR BioMuta; AFM; -.
DR DMDM; 1168366; -.
DR CPTAC; CPTAC-649; -.
DR CPTAC; CPTAC-650; -.
DR CPTAC; non-CPTAC-1058; -.
DR CPTAC; non-CPTAC-1059; -.
DR CPTAC; non-CPTAC-1060; -.
DR jPOST; P43652; -.
DR MassIVE; P43652; -.
DR PaxDb; P43652; -.
DR PeptideAtlas; P43652; -.
DR PRIDE; P43652; -.
DR ProteomicsDB; 55647; -.
DR ABCD; P43652; 1 sequenced antibody.
DR Antibodypedia; 1356; 269 antibodies from 33 providers.
DR DNASU; 173; -.
DR Ensembl; ENST00000226355.5; ENSP00000226355.3; ENSG00000079557.5.
DR GeneID; 173; -.
DR KEGG; hsa:173; -.
DR MANE-Select; ENST00000226355.5; ENSP00000226355.3; NM_001133.2; NP_001124.1.
DR UCSC; uc003hhb.4; human.
DR CTD; 173; -.
DR DisGeNET; 173; -.
DR GeneCards; AFM; -.
DR HGNC; HGNC:316; AFM.
DR HPA; ENSG00000079557; Tissue enriched (liver).
DR MIM; 104145; gene.
DR neXtProt; NX_P43652; -.
DR OpenTargets; ENSG00000079557; -.
DR PharmGKB; PA24613; -.
DR VEuPathDB; HostDB:ENSG00000079557; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR GeneTree; ENSGT00390000000113; -.
DR HOGENOM; CLU_030161_2_0_1; -.
DR InParanoid; P43652; -.
DR OMA; FAFRRHC; -.
DR OrthoDB; 906547at2759; -.
DR PhylomeDB; P43652; -.
DR TreeFam; TF335561; -.
DR PathwayCommons; P43652; -.
DR SignaLink; P43652; -.
DR BioGRID-ORCS; 173; 41 hits in 1063 CRISPR screens.
DR ChiTaRS; AFM; human.
DR GeneWiki; Afamin; -.
DR GenomeRNAi; 173; -.
DR Pharos; P43652; Tbio.
DR PRO; PR:P43652; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P43652; protein.
DR Bgee; ENSG00000079557; Expressed in right lobe of liver and 53 other tissues.
DR Genevisible; P43652; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0008431; F:vitamin E binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0071693; P:protein transport within extracellular region; IMP:UniProtKB.
DR GO; GO:0051180; P:vitamin transport; IDA:UniProtKB.
DR CDD; cd00015; ALBUMIN; 3.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR021177; Serum_albumin/AFP/Afamin.
DR InterPro; IPR020857; Serum_albumin_CS.
DR InterPro; IPR014760; Serum_albumin_N.
DR PANTHER; PTHR11385; PTHR11385; 1.
DR Pfam; PF00273; Serum_albumin; 3.
DR PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
DR PRINTS; PR00803; AFETOPROTEIN.
DR PRINTS; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 3.
DR SUPFAM; SSF48552; SSF48552; 3.
DR PROSITE; PS00212; ALBUMIN_1; 3.
DR PROSITE; PS51438; ALBUMIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protein transport; Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15952736"
FT CHAIN 22..599
FT /note="Afamin"
FT /id="PRO_0000001106"
FT DOMAIN 22..210
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 211..403
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 404..599
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT REGION 215..319
FT /note="Binding pocket for hydrophobic ligands"
FT /evidence="ECO:0000269|PubMed:29153507"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19838169"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) (complex) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19838169"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:26902720"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:26902720"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 99..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 113..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 148..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 192..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 224..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 269..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 289..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 302..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 340..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 461..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 483..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 498..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 536..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT DISULFID 580..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:29153507"
FT VARIANT 395
FT /note="R -> H (in dbSNP:rs41265665)"
FT /id="VAR_061003"
FT VARIANT 404
FT /note="T -> S (in dbSNP:rs2276444)"
FT /id="VAR_048218"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:6FAK"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6RQ7"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:6FAK"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 198..230
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 252..271
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:6FAK"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6FAK"
FT TURN 300..304
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:6FAK"
FT TURN 331..335
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 397..438
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 444..461
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 467..483
FT /evidence="ECO:0007829|PDB:6FAK"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 493..500
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 506..511
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:6FAK"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:6FAK"
FT HELIX 563..581
FT /evidence="ECO:0007829|PDB:6FAK"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:5OKL"
FT HELIX 586..593
FT /evidence="ECO:0007829|PDB:6FAK"
SQ SEQUENCE 599 AA; 69069 MW; D594E75E20D308AB CRC64;
MKLLKLTGFI FFLFFLTESL TLPTQPRDIE NFNSTQKFIE DNIEYITIIA FAQYVQEATF
EEMEKLVKDM VEYKDRCMAD KTLPECSKLP NNVLQEKICA MEGLPQKHNF SHCCSKVDAQ
RRLCFFYNKK SDVGFLPPFP TLDPEEKCQA YESNRESLLN HFLYEVARRN PFVFAPTLLT
VAVHFEEVAK SCCEEQNKVN CLQTRAIPVT QYLKAFSSYQ KHVCGALLKF GTKVVHFIYI
AILSQKFPKI EFKELISLVE DVSSNYDGCC EGDVVQCIRD TSKVMNHICS KQDSISSKIK
ECCEKKIPER GQCIINSNKD DRPKDLSLRE GKFTDSENVC QERDADPDTF FAKFTFEYSR
RHPDLSIPEL LRIVQIYKDL LRNCCNTENP PGCYRYAEDK FNETTEKSLK MVQQECKHFQ
NLGKDGLKYH YLIRLTKIAP QLSTEELVSL GEKMVTAFTT CCTLSEEFAC VDNLADLVFG
ELCGVNENRT INPAVDHCCK TNFAFRRPCF ESLKADKTYV PPPFSQDLFT FHADMCQSQN
EELQRKTDRF LVNLVKLKHE LTDEELQSLF TNFANVVDKC CKAESPEVCF NEESPKIGN
