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Afamin (Alpha-albumin)

 AFAM_BOVIN              Reviewed;         604 AA.
G3MYZ3;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
16-NOV-2011, sequence version 1.
20-JUN-2018, entry version 38.
RecName: Full=Afamin {ECO:0000303|PubMed:26902720};
AltName: Full=Alpha-albumin {ECO:0000303|PubMed:26902720};
Flags: Precursor;
Name=AFM {ECO:0000312|Ensembl:ENSBTAP00000054782};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913 {ECO:0000312|Proteomes:UP000009136};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hereford;
PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
"A whole-genome assembly of the domestic cow, Bos taurus.";
Genome Biol. 10:R42.01-R42.10(2009).
[2]
PROTEIN SEQUENCE OF 22-31, FUNCTION, INTERACTION WITH WNT3A AND WNT5A,
AND SUBCELLULAR LOCATION.
PubMed=26902720; DOI=10.7554/eLife.11621;
Mihara E., Hirai H., Yamamoto H., Tamura-Kawakami K., Matano M.,
Kikuchi A., Sato T., Takagi J.;
"Active and water-soluble form of lipidated Wnt protein is maintained
by a serum glycoprotein afamin/alpha-albumin.";
Elife 5:0-0(2016).
-!- FUNCTION: Functions as carrier for hydrophobic molecules in body
fluids. Essential for the solubility and activity of lipidated Wnt
family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A,
WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (PubMed:26902720).
Binds vitamin E. May transport vitamin E in body fluids under
conditions where the lipoprotein system is not sufficient. May be
involved in the transport of vitamin E across the blood-brain
barrier (By similarity). {ECO:0000250|UniProtKB:P43652,
ECO:0000269|PubMed:26902720}.
-!- SUBUNIT: Forms a 1:1 complex with Wnt family members; interacts
with WNT3A and WNT5A (PubMed:26902720). Interacts with WNT1,
WNT2B, WNT3, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B
(By similarity). {ECO:0000250|UniProtKB:P43652,
ECO:0000269|PubMed:26902720}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P43652}.
-!- DOMAIN: The second albumin domain forms a deep binding pocket that
contains palmitoleic acid (in vitro). Palmitoleic acid is most
likely not the physiological ligand. Instead, this pocket may
accomodate the covalently bound lipid moiety of Wnt family
members. {ECO:0000250|UniProtKB:P43652}.
-!- PTM: N-glycosylated; more than 90% of the glycans are sialylated.
{ECO:0000250|UniProtKB:P43652}.
-!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
{ECO:0000255|PROSITE-ProRule:PRU00769}.
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EMBL; DAAA02018076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001179104.1; NM_001192175.1.
RefSeq; XP_015327164.1; XM_015471678.1.
UniGene; Bt.14568; -.
ProteinModelPortal; G3MYZ3; -.
SMR; G3MYZ3; -.
STRING; 9913.ENSBTAP00000054782; -.
PaxDb; G3MYZ3; -.
PRIDE; G3MYZ3; -.
Ensembl; ENSBTAT00000063031; ENSBTAP00000054782; ENSBTAG00000047833.
GeneID; 508264; -.
KEGG; bta:508264; -.
CTD; 173; -.
VGNC; VGNC:25715; AFM.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
GeneTree; ENSGT00390000000113; -.
InParanoid; G3MYZ3; -.
OMA; LDPEEKC; -.
OrthoDB; EOG091G0F5F; -.
TreeFam; TF335561; -.
Proteomes; UP000009136; Chromosome 6.
Bgee; ENSBTAG00000047833; -.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0008431; F:vitamin E binding; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0071693; P:protein transport within extracellular region; ISS:UniProtKB.
GO; GO:0051180; P:vitamin transport; IEA:Ensembl.
CDD; cd00015; ALBUMIN; 3.
InterPro; IPR000264; ALB/AFP/VDB.
InterPro; IPR020858; Serum_albumin-like.
InterPro; IPR021177; Serum_albumin/AFP/Afamin.
InterPro; IPR020857; Serum_albumin_CS.
InterPro; IPR014760; Serum_albumin_N.
PANTHER; PTHR11385; PTHR11385; 1.
Pfam; PF00273; Serum_albumin; 3.
PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
PRINTS; PR00803; AFETOPROTEIN.
PRINTS; PR00802; SERUMALBUMIN.
SMART; SM00103; ALBUMIN; 3.
SUPFAM; SSF48552; SSF48552; 3.
PROSITE; PS00212; ALBUMIN_1; 3.
PROSITE; PS51438; ALBUMIN_2; 3.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Protein transport; Reference proteome; Repeat; Secreted;
Signal; Transport.
SIGNAL 1 21 {ECO:0000269|PubMed:26902720}.
CHAIN 22 604 Afamin.
/FTId=PRO_5003447762.
DOMAIN 22 210 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 211 403 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 404 598 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
REGION 215 319 Binding pocket for hydrophobic ligands.
{ECO:0000250|UniProtKB:P43652}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 434 434 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 77 86 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 99 114 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 113 124 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 148 193 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 192 201 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 224 270 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 269 277 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 289 303 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 302 313 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 340 385 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 384 393 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 416 462 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 461 470 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 483 499 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 498 509 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 536 581 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 580 589 {ECO:0000255|PROSITE-ProRule:PRU00769}.
SEQUENCE 604 AA; 69562 MW; CD5D1A0F2F9488B2 CRC64;
MKQLKLTGFV IFFFFLTESL TLPTQPQDVD DVRITQKFID DNIGYITIIA FAQYIQEASF
EEVEMLVKAM TEYRDKCLAD RTLPECSKLA NEVLLENICA MEGLPQKYNF SHCCHKVDFE
RRLCFFHNKK ADIGLLPPLP TLDPEEKCQT YKNNRESFLN NYVYEVSRRN PFVFAPTLLT
VAARFEEMTK TCCEEQEKAN CFQTKAEPFI YYLKALSSYQ KNACRALMKF GRQILQSINI
AILSQKFPKI GFKQLTSLLE DVSSKYDGCC EGDVVQCIRG RSKVMSHICS KQDSISSKIK
DCCEKKIPER GECIIYSNKD DRPNDLSLRE AKFIESDNVC EKRDADQANF MAEFLYEYSR
RHPELSTPEL LRIAKVYKDL LKECCNMENP PECYRHAENR FNETTEKSLK IVQRECEHFQ
NLGKDDLKYH YLINLTKLAP QLSTEELTFL GKEMVMALTT CCTLSEEFAC VDNLVDLVLG
ELCGINENRN INPAVDHCCK TNFAFRRSCF ESLEADKTYV PPSTSQGLFT FHADLCQAHN
EELQRKKDRF LVNLVKLKPE LAGEELWSLL ADFTNVVEKC CKAQEPEACF KEESPKLAAK
SQAA


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