AFAM_MOUSE
ID AFAM_MOUSE Reviewed; 608 AA.
AC O89020; Q3UNV0; Q497E6; Q8R0J9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Afamin;
DE AltName: Full=Alpha-albumin;
DE Short=Alpha-Alb;
DE Flags: Precursor;
GN Name=Afm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Diaphragm;
RA van Reeth T., Gabant P., Dreze P., Szpirer J., Szpirer C.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 18-608 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-402.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-153 AND ASN-402.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH WNT3A.
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).
CC -!- FUNCTION: Functions as carrier for hydrophobic molecules in body
CC fluids. 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. Binds vitamin E. May
CC transport vitamin E in body fluids under conditions where the
CC lipoprotein system is not sufficient. May be involved in the transport
CC of vitamin E across the blood-brain barrier.
CC {ECO:0000250|UniProtKB:P43652}.
CC -!- SUBUNIT: Forms a 1:1 complex with Wnt family members; interacts with
CC WNT1, WNT2B, WNT3, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and
CC WNT10B (By similarity). Interacts with WNT3A (PubMed:26902720).
CC {ECO:0000250|UniProtKB:P43652, ECO:0000269|PubMed:26902720}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P43652}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O89020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O89020-2; Sequence=VSP_023387, VSP_023388;
CC Name=3;
CC IsoId=O89020-3; Sequence=VSP_023389;
CC -!- TISSUE SPECIFICITY: Detected in brain, especially on brain capillaries
CC (at protein level). Expressed in isolated brain capillaries.
CC {ECO:0000269|PubMed:19046407}.
CC -!- DOMAIN: The second albumin domain forms a deep binding pocket that
CC contains palmitoleic acid (in vitro). Palmitoleic acid is most likely
CC not the physiological ligand. Instead, this pocket may accomodate the
CC covalently bound lipid moiety of Wnt family members.
CC {ECO:0000250|UniProtKB:P43652}.
CC -!- PTM: N-glycosylated; more than 90% of the glycans are sialylated.
CC {ECO:0000250|UniProtKB:P43652}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26681.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AJ011080; CAA09471.1; -; mRNA.
DR EMBL; AK143987; BAE25647.1; -; mRNA.
DR EMBL; BC026681; AAH26681.1; ALT_SEQ; mRNA.
DR EMBL; BC100597; AAI00598.1; -; mRNA.
DR CCDS; CCDS39141.1; -. [O89020-1]
DR RefSeq; NP_660128.2; NM_145146.2. [O89020-1]
DR AlphaFoldDB; O89020; -.
DR SMR; O89020; -.
DR STRING; 10090.ENSMUSP00000108804; -.
DR GlyGen; O89020; 5 sites.
DR iPTMnet; O89020; -.
DR PhosphoSitePlus; O89020; -.
DR CPTAC; non-CPTAC-3328; -.
DR MaxQB; O89020; -.
DR PaxDb; O89020; -.
DR PeptideAtlas; O89020; -.
DR PRIDE; O89020; -.
DR ProteomicsDB; 281950; -. [O89020-1]
DR ProteomicsDB; 281951; -. [O89020-2]
DR ProteomicsDB; 281952; -. [O89020-3]
DR Antibodypedia; 1356; 269 antibodies from 33 providers.
DR DNASU; 280662; -.
DR Ensembl; ENSMUST00000113179; ENSMUSP00000108804; ENSMUSG00000029369. [O89020-1]
DR Ensembl; ENSMUST00000128740; ENSMUSP00000117180; ENSMUSG00000029369. [O89020-2]
DR GeneID; 280662; -.
DR KEGG; mmu:280662; -.
DR UCSC; uc008ybb.1; mouse. [O89020-2]
DR UCSC; uc008ybc.1; mouse. [O89020-1]
DR CTD; 173; -.
DR MGI; MGI:2429409; Afm.
DR VEuPathDB; HostDB:ENSMUSG00000029369; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR GeneTree; ENSGT00390000000113; -.
DR HOGENOM; CLU_030161_2_0_1; -.
DR InParanoid; O89020; -.
DR OMA; FAFRRHC; -.
DR OrthoDB; 906547at2759; -.
DR PhylomeDB; O89020; -.
DR TreeFam; TF335561; -.
DR BioGRID-ORCS; 280662; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Afm; mouse.
DR PRO; PR:O89020; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O89020; protein.
DR Bgee; ENSMUSG00000029369; Expressed in left lobe of liver and 55 other tissues.
DR Genevisible; O89020; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0008431; F:vitamin E binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0071693; P:protein transport within extracellular region; ISS:UniProtKB.
DR GO; GO:0051180; P:vitamin transport; ISS: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; 2.
DR PROSITE; PS51438; ALBUMIN_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Protein transport;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P43652"
FT CHAIN 22..608
FT /note="Afamin"
FT /id="PRO_0000001107"
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:0000250|UniProtKB:P43652"
FT REGION 583..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941, ECO:0000269|PubMed:19159218"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941, ECO:0000269|PubMed:19159218"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 99..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 113..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 148..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 192..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 224..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 269..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 289..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 302..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 340..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 461..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 483..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 498..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 580..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT VAR_SEQ 430
FT /note="H -> Q (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023387"
FT VAR_SEQ 431..608
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023388"
FT VAR_SEQ 606..608
FT /note="KQR -> NKITDQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023389"
FT CONFLICT 44
FT /note="T -> A (in Ref. 1; CAA09471 and 3; AAH26681)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="N -> K (in Ref. 1; CAA09471)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="S -> N (in Ref. 3; AAI00598)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="V -> E (in Ref. 1; CAA09471)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="I -> V (in Ref. 3; AAI00598)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="T -> I (in Ref. 3; AAI00598)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="E -> R (in Ref. 1; CAA09471)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="K -> N (in Ref. 1; CAA09471)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="E -> A (in Ref. 1; CAA09471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 69379 MW; 98B31E6D96E73F12 CRC64;
MRHLKLTGFI FFLLPLTESL ALPTKPQDVD HFNATQKFID ENTTYLAIIA FSQYVQEASF
DEVETLVKVM LDYRDRCWAD NTLPECSKTA NDAIQDMLCD MEGLPQKHNF SHCCGKAGFP
RRLCFFYNKK ANVGFLPPFP TLDPEEKCQA YKNNSESFLH LYMYEVARRN PFVFAPVLLA
VAAWFEEAAT TCCEQQQKAT CFQAKAAPIT QYLKASSSYQ RNVCGALIKF GPKVLNSINV
AVFSKKFPKI GFKDLTTLLE DVSSMYEGCC EGDVVHCIRS QSQVVNHICS KQDSISSKIK
VCCEKKTLER EACIINANKD DRPEGLSLRE AKFTESENVC QERDSDPDKF FAEFIYEYSR
RHPDLSTPEL LRITKVYMDF LEDCCSRENP AGCYRHVEDK FNETTQRSLA MVQQECKQFQ
ELGKDTLQRH FLVKFTKAAP QLPMEELVSL SKEMVAALTT CCTLSDEFAC VDNLADLVLG
ELCGVNTNRT INPAVDHCCK TDFAFRRHCF EHLKADTTYE LPSVSALVSA LHTDWCQPRK
EDLQNKKHRF LVNLVKWMPG ITDEEWLCLF TKFTAAREEC SEVQEPESCF SPESSKTGDE
SQATEKQR
