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Afamin (Alpha-albumin) (Alpha-Alb)

 AFAM_MOUSE              Reviewed;         608 AA.
O89020; Q3UNV0; Q497E6; Q8R0J9;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
10-MAY-2017, entry version 123.
RecName: Full=Afamin;
AltName: Full=Alpha-albumin;
Short=Alpha-Alb;
Flags: Precursor;
Name=Afm;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Diaphragm;
van Reeth T., Gabant P., Dreze P., Szpirer J., Szpirer C.;
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 18-608 (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Kidney, and Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-402.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-153 AND ASN-402.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[6]
TISSUE SPECIFICITY.
PubMed=19046407; DOI=10.1111/j.1471-4159.2008.05796.x;
Kratzer I., Bernhart E., Wintersperger A., Hammer A., Waltl S.,
Malle E., Sperk G., Wietzorrek G., Dieplinger H., Sattler W.;
"Afamin is synthesized by cerebrovascular endothelial cells and
mediates alpha-tocopherol transport across an in vitro model of the
blood-brain barrier.";
J. Neurochem. 108:707-718(2009).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-402.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Vitamin E binding protein. May transport vitamin E in
body fluids under conditions where the lipoprotein system is not
sufficient or across the blood-brain barrier (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Note=Detected in large and small
blood vessels throughout the cortex and the striatum.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O89020-1; Sequence=Displayed;
Name=2;
IsoId=O89020-2; Sequence=VSP_023387, VSP_023388;
Name=3;
IsoId=O89020-3; Sequence=VSP_023389;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in brain (at protein level).
Expressed in isolated brain capillaries.
{ECO:0000269|PubMed:19046407}.
-!- PTM: N-glycosylated; more than 90% of the glycans are sialylated.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
{ECO:0000255|PROSITE-ProRule:PRU00769}.
-!- SEQUENCE CAUTION:
Sequence=AAH26681.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ011080; CAA09471.1; -; mRNA.
EMBL; AK143987; BAE25647.1; -; mRNA.
EMBL; BC026681; AAH26681.1; ALT_SEQ; mRNA.
EMBL; BC100597; AAI00598.1; -; mRNA.
CCDS; CCDS39141.1; -. [O89020-1]
RefSeq; NP_660128.2; NM_145146.2. [O89020-1]
UniGene; Mm.348786; -.
ProteinModelPortal; O89020; -.
SMR; O89020; -.
IntAct; O89020; 1.
MINT; MINT-4087327; -.
STRING; 10090.ENSMUSP00000108804; -.
iPTMnet; O89020; -.
PhosphoSitePlus; O89020; -.
MaxQB; O89020; -.
PaxDb; O89020; -.
PeptideAtlas; O89020; -.
PRIDE; O89020; -.
Ensembl; ENSMUST00000113179; ENSMUSP00000108804; ENSMUSG00000029369. [O89020-1]
Ensembl; ENSMUST00000128740; ENSMUSP00000117180; ENSMUSG00000029369. [O89020-2]
GeneID; 280662; -.
KEGG; mmu:280662; -.
UCSC; uc008ybb.1; mouse. [O89020-2]
UCSC; uc008ybc.1; mouse. [O89020-1]
CTD; 173; -.
MGI; MGI:2429409; Afm.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
GeneTree; ENSGT00390000000113; -.
HOGENOM; HOG000293137; -.
HOVERGEN; HBG004207; -.
InParanoid; O89020; -.
OMA; LDPEEKC; -.
OrthoDB; EOG091G0F5F; -.
PhylomeDB; O89020; -.
TreeFam; TF335561; -.
ChiTaRS; Afm; mouse.
PRO; PR:O89020; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029369; -.
CleanEx; MM_AFM; -.
Genevisible; O89020; MM.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0008431; F:vitamin E binding; ISS:UniProtKB.
GO; GO:0051180; P:vitamin transport; ISS:UniProtKB.
CDD; cd00015; ALBUMIN; 3.
InterPro; IPR000264; ALB/AFP/VDB.
InterPro; IPR020858; Serum_albumin-like.
InterPro; IPR021177; Serum_albumin/AFP/Afamin.
InterPro; IPR020857; Serum_albumin_CS.
InterPro; IPR014760; Serum_albumin_N.
PANTHER; PTHR11385; PTHR11385; 1.
Pfam; PF00273; Serum_albumin; 3.
PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
PRINTS; PR00803; AFETOPROTEIN.
PRINTS; PR00802; SERUMALBUMIN.
SMART; SM00103; ALBUMIN; 3.
SUPFAM; SSF48552; SSF48552; 3.
PROSITE; PS00212; ALBUMIN_1; 2.
PROSITE; PS51438; ALBUMIN_2; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 21 {ECO:0000250}.
CHAIN 22 608 Afamin.
/FTId=PRO_0000001107.
DOMAIN 22 210 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 211 403 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 404 599 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:17330941,
ECO:0000269|PubMed:19159218}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:17330941,
ECO:0000269|PubMed:19159218}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 77 86 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 99 114 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 113 124 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 148 193 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 224 270 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 269 277 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 289 303 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 302 313 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 340 385 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 384 393 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 416 462 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 461 470 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 483 499 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 498 509 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 580 589 {ECO:0000255|PROSITE-ProRule:PRU00769}.
VAR_SEQ 430 430 H -> Q (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_023387.
VAR_SEQ 431 608 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_023388.
VAR_SEQ 606 608 KQR -> NKITDQ (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_023389.
CONFLICT 44 44 T -> A (in Ref. 1; CAA09471 and 3;
AAH26681). {ECO:0000305}.
CONFLICT 154 154 N -> K (in Ref. 1; CAA09471).
{ECO:0000305}.
CONFLICT 280 280 S -> N (in Ref. 3; AAI00598).
{ECO:0000305}.
CONFLICT 285 285 V -> E (in Ref. 1; CAA09471).
{ECO:0000305}.
CONFLICT 295 295 I -> V (in Ref. 3; AAI00598).
{ECO:0000305}.
CONFLICT 307 307 T -> I (in Ref. 3; AAI00598).
{ECO:0000305}.
CONFLICT 369 369 E -> R (in Ref. 1; CAA09471).
{ECO:0000305}.
CONFLICT 417 417 K -> N (in Ref. 1; CAA09471).
{ECO:0000305}.
CONFLICT 520 520 E -> A (in Ref. 1; CAA09471).
{ECO:0000305}.
SEQUENCE 608 AA; 69379 MW; 98B31E6D96E73F12 CRC64;
MRHLKLTGFI FFLLPLTESL ALPTKPQDVD HFNATQKFID ENTTYLAIIA FSQYVQEASF
DEVETLVKVM LDYRDRCWAD NTLPECSKTA NDAIQDMLCD MEGLPQKHNF SHCCGKAGFP
RRLCFFYNKK ANVGFLPPFP TLDPEEKCQA YKNNSESFLH LYMYEVARRN PFVFAPVLLA
VAAWFEEAAT TCCEQQQKAT CFQAKAAPIT QYLKASSSYQ RNVCGALIKF GPKVLNSINV
AVFSKKFPKI GFKDLTTLLE DVSSMYEGCC EGDVVHCIRS QSQVVNHICS KQDSISSKIK
VCCEKKTLER EACIINANKD DRPEGLSLRE AKFTESENVC QERDSDPDKF FAEFIYEYSR
RHPDLSTPEL LRITKVYMDF LEDCCSRENP AGCYRHVEDK FNETTQRSLA MVQQECKQFQ
ELGKDTLQRH FLVKFTKAAP QLPMEELVSL SKEMVAALTT CCTLSDEFAC VDNLADLVLG
ELCGVNTNRT INPAVDHCCK TDFAFRRHCF EHLKADTTYE LPSVSALVSA LHTDWCQPRK
EDLQNKKHRF LVNLVKWMPG ITDEEWLCLF TKFTAAREEC SEVQEPESCF SPESSKTGDE
SQATEKQR


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