ID   ALBU2_SALSA             Reviewed;         608 AA.
AC   Q03156;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Albumin 2;
DE   Flags: Precursor;
GN   Name=alb2;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1398147; DOI=10.1016/0378-1119(92)90115-6;
RA   Byrnes L., Gannon F.;
RT   "Sequence analysis of a second cDNA encoding Atlantic salmon (Salmo salar)
RT   serum albumin.";
RL   Gene 120:319-320(1992).
CC   -!- FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones,
CC       bilirubin and drugs. Its main function is the regulation of the
CC       colloidal osmotic pressure of blood.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00769}.
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DR   EMBL; X60776; CAA43187.1; -; mRNA.
DR   PIR; A46757; ABONS2.
DR   RefSeq; NP_001117164.1; NM_001123692.1.
DR   AlphaFoldDB; Q03156; -.
DR   SMR; Q03156; -.
DR   GeneID; 100136922; -.
DR   KEGG; sasa:100136922; -.
DR   OrthoDB; 906547at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa18.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR   PROSITE; PS51438; ALBUMIN_2; 3.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Lipid-binding; Metal-binding;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   PROPEP          15..18
FT                   /id="PRO_0000001087"
FT   CHAIN           19..608
FT                   /note="Albumin 2"
FT                   /id="PRO_0000001088"
FT   DOMAIN          19..205
FT                   /note="Albumin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          206..398
FT                   /note="Albumin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          402..600
FT                   /note="Albumin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        93..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        107..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        142..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        186..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        218..264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        263..271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        283..299
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        298..309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        336..381
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        380..389
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        414..460
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        459..471
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        484..500
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        499..510
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        537..582
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        581..590
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ   SEQUENCE   608 AA;  67059 MW;  C168DD349F4E16C5 CRC64;
     MQWLSVCSLL VLLSVLSRSQ AQNQICTIFT EAKEDGFKSL ILVGLAQNLP DSTLGDLVPL
     IAEALAMGVK CCSDTPPEDC ERDVADLFQS AVCSSETLVE KNDLKMCCEK TAAERTHCFV
     DHKAKIPRDL SLKAELPAAD QCEDFKKDHK AFVGRFIFKF SKSNPMLPPH VVLAIAKGYG
     EVLTTCCGEA EAQTCFDTKK ATFQHAIAKR VAELKSLCIV HKKYGDRVVK AKKLVQYSQK
     MPQASFQEMA GMVDKIVATV APCCSGDMVT CMKERKTLVD EVCADESVLS RAAGLSACCK
     EDAVHRGSCV EAMKPDPKPD GLSEHYDVHA DIAAVCQTFT KTPDVAMGKL VYEISVRHPE
     SSQQVILRFA KEAEQALLQC CDMEDHAECV KTALAGSDID KKITDETDYY KKMCAAEAAV
     SDDNFEKSMM VYYTRIMPQA SFDQLHMVSE TVHDVLHACC KDEPGHFVLP CAEEKLTDAI
     DATCDDYDPS SINPHIAHCC NQSYSMRRHC ILAIQPDTEF TPPELDASSF HMGPELCTKD
     SKDLLLSGKK LLYGVVRHKT TITEDHLKTI STKYHTMKDK CCAAEDQAAC FTEEAPKLVS
     ESAELVKV