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   24-JAN-2024, entry version 118.
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 a 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   GlyCosmos; P36953; 5 sites, No reported glycans.
DR   GlyGen; P36953; 5 sites.
DR   iPTMnet; P36953; -.
DR   PhosphoSitePlus; P36953; -.
DR   PaxDb; 10116-ENSRNOP00000057275; -.
DR   GeneID; 282708; -.
DR   KEGG; rno:282708; -.
DR   UCSC; RGD:628614; rat.
DR   AGR; RGD:628614; -.
DR   CTD; 173; -.
DR   RGD; 628614; Afm.
DR   eggNOG; ENOG502R7EA; Eukaryota.
DR   InParanoid; P36953; -.
DR   OrthoDB; 5196468at2759; -.
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:0008431; F:vitamin E binding; ISS:UniProtKB.
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   Gene3D; 1.10.246.10; -; 6.
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:SF14; AFAMIN; 1.
DR   PANTHER; PTHR11385; SERUM ALBUMIN-RELATED; 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; Serum albumin-like; 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
//