SAA2_HUMAN
ID SAA2_HUMAN Reviewed; 122 AA.
AC P0DJI9; G3XAK9; P02735; P02736; P02737; Q16730; Q16834; Q16835; Q16879;
AC Q3KRB3; Q6FG67; Q96QN0; Q9UCK9; Q9UCL0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Serum amyloid A-2 protein {ECO:0000305};
DE Short=SAA2;
DE Contains:
DE RecName: Full=Amyloid A2 protein {ECO:0000303|PubMed:1463770};
DE Short=AA2 {ECO:0000303|PubMed:1463770};
DE Flags: Precursor;
GN Name=SAA2 {ECO:0000312|HGNC:HGNC:10514};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA2.1).
RX PubMed=3800865; DOI=10.1007/bf00554519;
RA Kluve-Beckerman B., Long G.L., Benson M.D.;
RT "DNA sequence evidence for polymorphic forms of human serum amyloid A
RT (SAA).";
RL Biochem. Genet. 24:795-803(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE SAA2.2), AND INDUCTION.
RX PubMed=2890635; DOI=10.1016/s0021-9258(18)47798-8;
RA Woo P., Sipe J., Dinarello C.A., Colten H.R.;
RT "Structure of a human serum amyloid A gene and modulation of its expression
RT in transfected L cells.";
RL J. Biol. Chem. 262:15790-15795(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES SAA2.1 AND SAA2.2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=3183061; DOI=10.1172/jci113779;
RA Kluve-Beckerman B., Dwulet F.E., Benson M.D.;
RT "Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins
RT in one person.";
RL J. Clin. Invest. 82:1670-1675(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA2.1).
RC TISSUE=Liver;
RX PubMed=1971508; DOI=10.1042/bj2680187;
RA Steinkasserer A., Weiss E.H., Schwaeble W., Linke R.P.;
RT "Heterogeneity of human serum amyloid A protein. Five different variants
RT from one individual demonstrated by cDNA sequence analysis.";
RL Biochem. J. 268:187-193(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE SAA2.2).
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA2.1).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 19-94, DISEASE, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND VARIANT HIS-89.
RC TISSUE=Thyroid;
RX PubMed=1463770; DOI=10.1016/0925-4439(92)90068-x;
RA Baba S., Takahashi T., Kasama T., Shirasawa H.;
RT "Identification of two novel amyloid A protein subsets coexisting in an
RT individual patient of AA-amyloidosis.";
RL Biochim. Biophys. Acta 1180:195-200(1992).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-122, AND VARIANT HIS-89.
RC TISSUE=Liver;
RX PubMed=1656519; DOI=10.1111/j.1365-3083.1991.tb01570.x;
RA Betts J., Edbrooke M., Thakker R., Woo P.;
RT "The human acute-phase serum amyloid A gene family: structure, evolution
RT and expression in hepatoma cells.";
RL Scand. J. Immunol. 34:471-482(1991).
RN [11]
RP POLYMORPHISM, AND NOMENCLATURE OF ALLELES.
RX PubMed=10211414; DOI=10.3109/13506129908993291;
RA Sipe J.;
RT "Revised nomenclature for serum amyloid A (SAA). Nomenclature Committee of
RT the International Society of Amyloidosis. Part 2.";
RL Amyloid 6:67-70(1999).
CC -!- FUNCTION: Major acute phase reactant. {ECO:0000250|UniProtKB:P05366}.
CC -!- SUBUNIT: Apolipoprotein of the HDL complex.
CC {ECO:0000250|UniProtKB:P0DJI8}.
CC -!- INTERACTION:
CC P0DJI9; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-6677144, EBI-7062247;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DJI8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DJI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DJI9-2; Sequence=VSP_045626;
CC -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC {ECO:0000269|PubMed:3183061}.
CC -!- INDUCTION: Upon cytokine stimulation. {ECO:0000269|PubMed:2890635}.
CC -!- POLYMORPHISM: At least 2 different SAA2 alleles have been described:
CC SAA2.1 (SAA2alpha) and SAA2.2 (SAA2beta). We use here the revised
CC nomenclature described in PubMed:10211414. The sequence shown is that
CC of SAA2.2. {ECO:0000305|PubMed:10211414}.
CC -!- DISEASE: Note=Reactive, secondary amyloidosis is characterized by the
CC extracellular accumulation in various tissues of the SAA2 protein.
CC These deposits are highly insoluble and resistant to proteolysis; they
CC disrupt tissue structure and compromise function.
CC {ECO:0000269|PubMed:1463770}.
CC -!- SIMILARITY: Belongs to the SAA family. {ECO:0000305}.
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DR EMBL; M26152; AAA85338.1; -; mRNA.
DR EMBL; J03474; AAB59539.1; -; Genomic_DNA.
DR EMBL; M23699; AAA64800.1; -; mRNA.
DR EMBL; M23700; AAA64801.1; -; mRNA.
DR EMBL; X51440; CAA35805.1; -; mRNA.
DR EMBL; X51444; CAA35809.1; -; mRNA.
DR EMBL; X51445; CAA35810.1; -; mRNA.
DR EMBL; X56653; CAA39975.1; -; Genomic_DNA.
DR EMBL; AK307163; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC090099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68414.1; -; Genomic_DNA.
DR EMBL; BC020795; AAH20795.1; -; mRNA.
DR CCDS; CCDS44548.1; -. [P0DJI9-2]
DR CCDS; CCDS7833.1; -. [P0DJI9-1]
DR RefSeq; NP_001120852.1; NM_001127380.2. [P0DJI9-2]
DR RefSeq; NP_110381.2; NM_030754.4. [P0DJI9-1]
DR AlphaFoldDB; P0DJI9; -.
DR SMR; P0DJI9; -.
DR BioGRID; 112197; 7.
DR IntAct; P0DJI9; 2.
DR STRING; 9606.ENSP00000436126; -.
DR GlyGen; P0DJI9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0DJI9; -.
DR PhosphoSitePlus; P0DJI9; -.
DR BioMuta; SAA2; -.
DR DMDM; 395406827; -.
DR EPD; P0DJI9; -.
DR jPOST; P0DJI9; -.
DR MassIVE; P0DJI9; -.
DR PaxDb; P0DJI9; -.
DR PeptideAtlas; P0DJI9; -.
DR PRIDE; P0DJI9; -.
DR ProteomicsDB; 33775; -.
DR ProteomicsDB; 52550; -. [P0DJI9-1]
DR Antibodypedia; 24987; 64 antibodies from 18 providers.
DR DNASU; 6289; -.
DR Ensembl; ENST00000256733.9; ENSP00000256733.5; ENSG00000134339.9. [P0DJI9-1]
DR Ensembl; ENST00000414546.6; ENSP00000416716.2; ENSG00000134339.9. [P0DJI9-2]
DR Ensembl; ENST00000526900.1; ENSP00000436126.1; ENSG00000134339.9. [P0DJI9-1]
DR Ensembl; ENST00000529528.5; ENSP00000437162.1; ENSG00000134339.9. [P0DJI9-1]
DR GeneID; 6289; -.
DR KEGG; hsa:6289; -.
DR MANE-Select; ENST00000256733.9; ENSP00000256733.5; NM_030754.5; NP_110381.2.
DR UCSC; uc001mnz.5; human. [P0DJI9-1]
DR CTD; 6289; -.
DR DisGeNET; 6289; -.
DR GeneCards; SAA2; -.
DR HGNC; HGNC:10514; SAA2.
DR HPA; ENSG00000134339; Tissue enriched (liver).
DR MIM; 104751; gene.
DR neXtProt; NX_P0DJI9; -.
DR OpenTargets; ENSG00000134339; -.
DR VEuPathDB; HostDB:ENSG00000134339; -.
DR eggNOG; ENOG502S4PB; Eukaryota.
DR GeneTree; ENSGT00390000004737; -.
DR HOGENOM; CLU_129936_0_0_1; -.
DR InParanoid; P0DJI9; -.
DR OMA; MREANWI; -.
DR OrthoDB; 1417043at2759; -.
DR PhylomeDB; P0DJI9; -.
DR TreeFam; TF332544; -.
DR PathwayCommons; P0DJI9; -.
DR SignaLink; P0DJI9; -.
DR BioGRID-ORCS; 6289; 13 hits in 981 CRISPR screens.
DR GeneWiki; SAA2; -.
DR GenomeRNAi; 6289; -.
DR Pharos; P0DJI9; Tbio.
DR PRO; PR:P0DJI9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P0DJI9; protein.
DR Bgee; ENSG00000134339; Expressed in right lobe of liver and 94 other tissues.
DR ExpressionAtlas; P0DJI9; baseline and differential.
DR Genevisible; P0DJI9; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR InterPro; IPR000096; Serum_amyloid_A.
DR Pfam; PF00277; SAA; 1.
DR PIRSF; PIRSF002472; Serum_amyloid_A; 1.
DR PRINTS; PR00306; SERUMAMYLOID.
DR SMART; SM00197; SAA; 1.
DR PROSITE; PS00992; SAA; 1.
PE 1: Evidence at protein level;
KW Acute phase; Alternative splicing; Amyloid; Amyloidosis;
KW Direct protein sequencing; HDL; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1463770"
FT CHAIN 19..122
FT /note="Serum amyloid A-2 protein"
FT /id="PRO_0000418061"
FT CHAIN 19..94
FT /note="Amyloid A2 protein"
FT /evidence="ECO:0000269|PubMed:1463770"
FT /id="PRO_0000450359"
FT REGION 88..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 78..122
FT /note="NARENIQRLTGRGAEDSLADQAANKWGRSGRDPNHFRPAGLPEKY -> LFS
FT AEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045626"
FT VARIANT 89
FT /note="R -> H (in allele SAA2.1; dbSNP:rs2229338)"
FT /evidence="ECO:0000269|PubMed:1463770,
FT ECO:0000269|PubMed:1656519"
FT /id="VAR_006930"
FT CONFLICT 15
FT /note="S -> G (in Ref. 2; AAB59539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 122 AA; 13527 MW; C4AAB684E0EDCBB8 CRC64;
MKLLTGLVFC SLVLSVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS DKYFHARGNY
DAAKRGPGGA WAAEVISNAR ENIQRLTGRG AEDSLADQAA NKWGRSGRDP NHFRPAGLPE
KY
