AFAM_RAT
ID AFAM_RAT Reviewed; 608 AA.
AC P36953;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Afamin;
DE AltName: Full=Alpha-albumin;
DE Short=Alpha-Alb;
DE Flags: Precursor;
GN Name=Afm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7509788; DOI=10.1016/s0021-9258(17)37482-3;
RA Belanger L., Roy S., Allard D.;
RT "New albumin gene 3' adjacent to the alpha 1-fetoprotein locus.";
RL J. Biol. Chem. 269:5481-5484(1994).
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, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B,
CC WNT10A and WNT10B. {ECO:0000250|UniProtKB:P43652}.
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; X76456; CAA53994.1; -; Genomic_DNA.
DR PIR; A53195; A53195.
DR RefSeq; NP_758823.1; NM_172320.1.
DR AlphaFoldDB; P36953; -.
DR SMR; P36953; -.
DR STRING; 10116.ENSRNOP00000057275; -.
DR GlyGen; P36953; 5 sites.
DR iPTMnet; P36953; -.
DR PhosphoSitePlus; P36953; -.
DR PaxDb; P36953; -.
DR PRIDE; P36953; -.
DR GeneID; 282708; -.
DR KEGG; rno:282708; -.
DR UCSC; RGD:628614; rat.
DR CTD; 173; -.
DR RGD; 628614; Afm.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P36953; -.
DR OrthoDB; 906547at2759; -.
DR PhylomeDB; P36953; -.
DR PRO; PR:P36953; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
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; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 3.
DR SUPFAM; SSF48552; SSF48552; 3.
DR PROSITE; PS00212; ALBUMIN_1; 1.
DR PROSITE; PS51438; ALBUMIN_2; 3.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Protein transport; Reference proteome;
KW Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P43652"
FT CHAIN 22..608
FT /note="Afamin"
FT /id="PRO_0000001108"
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 585..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 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"
SQ SEQUENCE 608 AA; 69335 MW; F33151A6E68A07F6 CRC64;
MRHLKLTGFI FFLLSLTESL ALPTKPQDVD HFNATQKFIN ENVAYLTIIA SAQYVQEASF
EEVEMLVKVM LDYKDRCLAD STLPECSKIA NDAIQDMLCD MKGLPQKHNF SHCCRQAGFQ
RRLCFFYNKK ANVGFLPPFP TLDPEEKCQA YKNNSESFLN LYMYEVARRN PFAFAPVLLN
VAARFEEAAT TCCEQQQKAT YFQDKAAPIT QYLKALSSYQ RNVCGALLKF GPKTLNSINI
AVFSKKFPKI GFEDLTSLLE DVSSMYDGCC EGDVVQCIRS QSQVMHHICS KQDSISSKIK
ACCEKKLPER ADCIINANKD DRPEDLSLRT PKFTDSENVC QERDSEQDKF FAEFLYDYSR
RHTELSTPEL LRITKVYKDL LEDCCNRKNP LSCYRHAEDK FNETTERSLA MVQQECKQFQ
ELGKDALQRH FLVKFTKAAP QLPMEELVSL SKEMVAALAT CCTLSDEFAC VDNLADLVLG
ELCGMNKNRT INPTVDHCCR ADFAFRRPCF EHLKADTTYA LPSVSALVSA LRADWCQPLK
EDLQNKRHRF LVNLVKWMPE ITDEERLCLF TKFTAAGEEC GNIQKPEACF SPESSKTGDV
SQDAEKQR
