AFAM_BOVIN
ID AFAM_BOVIN Reviewed; 604 AA.
AC G3MYZ3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Afamin {ECO:0000303|PubMed:26902720};
DE AltName: Full=Alpha-albumin {ECO:0000303|PubMed:26902720};
DE Flags: Precursor;
GN Name=AFM {ECO:0000312|Ensembl:ENSBTAP00000054782};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000312|Proteomes:UP000009136};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP PROTEIN SEQUENCE OF 22-31, FUNCTION, INTERACTION WITH WNT3A AND WNT5A, AND
RP SUBCELLULAR LOCATION.
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 (PubMed:26902720). Binds
CC vitamin E. May transport vitamin E in body fluids under conditions
CC where the lipoprotein system is not sufficient. May be involved in the
CC transport of vitamin E across the blood-brain barrier (By similarity).
CC {ECO:0000250|UniProtKB:P43652, ECO:0000269|PubMed:26902720}.
CC -!- SUBUNIT: Forms a 1:1 complex with Wnt family members; interacts with
CC WNT3A and WNT5A (PubMed:26902720). Interacts with WNT1, WNT2B, WNT3,
CC WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (By similarity).
CC {ECO:0000250|UniProtKB:P43652, ECO:0000269|PubMed:26902720}.
CC -!- INTERACTION:
CC G3MYZ3; P27467: Wnt3a; Xeno; NbExp=3; IntAct=EBI-22052138, EBI-2899665;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P43652}.
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}.
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DR EMBL; DAAA02018076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179104.1; NM_001192175.1.
DR RefSeq; XP_015327164.1; XM_015471678.1.
DR AlphaFoldDB; G3MYZ3; -.
DR SMR; G3MYZ3; -.
DR IntAct; G3MYZ3; 1.
DR STRING; 9913.ENSBTAP00000054782; -.
DR PaxDb; G3MYZ3; -.
DR Ensembl; ENSBTAT00000063031; ENSBTAP00000054782; ENSBTAG00000047833.
DR GeneID; 508264; -.
DR KEGG; bta:508264; -.
DR CTD; 173; -.
DR VEuPathDB; HostDB:ENSBTAG00000047833; -.
DR VGNC; VGNC:25715; AFM.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR GeneTree; ENSGT00390000000113; -.
DR HOGENOM; CLU_030161_2_0_1; -.
DR InParanoid; G3MYZ3; -.
DR OMA; FAFRRHC; -.
DR OrthoDB; 906547at2759; -.
DR TreeFam; TF335561; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000047833; Expressed in liver and 19 other tissues.
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; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0051180; P:vitamin transport; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Protein transport;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:26902720"
FT CHAIN 22..604
FT /note="Afamin"
FT /id="PRO_5003447762"
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..598
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 CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
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 536..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 580..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ 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
