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APOD_MOUSE
ID   APOD_MOUSE              Reviewed;         189 AA.
AC   P51910; Q3TZE7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Apolipoprotein D;
DE            Short=Apo-D;
DE            Short=ApoD;
DE   Flags: Precursor;
GN   Name=Apod;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=7637575; DOI=10.1016/0169-328x(95)00008-g;
RA   Seguin D., Desforges M., Rassart E.;
RT   "Molecular characterization and differential mRNA tissue distribution of
RT   mouse apolipoprotein D.";
RL   Brain Res. Mol. Brain Res. 30:242-250(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Mammary gland;
RX   PubMed=8666283; DOI=10.1016/0378-1119(96)00099-6;
RA   Cofer S., Ross R.R.;
RT   "The murine gene encoding apolipoprotein D exhibits a unique expression
RT   pattern as compared to other species.";
RL   Gene 171:261-263(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Diencephalon, Embryonic head, Inner ear, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: APOD occurs in the macromolecular complex with lecithin-
CC       transport and binding of bilin. Appears to be able to transport a
CC       variety of ligands in a number of different contexts.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highest levels of expression in brain, testis,
CC       virgin mammary gland and salivary gland. Moderate levels in skeletal
CC       muscle, lactating mammary gland and thymus. Low levels in lung and
CC       lymph node. No expression in kidney, pancreas, liver or spleen.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; L39123; AAA67892.1; -; Genomic_DNA.
DR   EMBL; X82648; CAA57974.1; -; mRNA.
DR   EMBL; AK135046; BAE22397.1; -; mRNA.
DR   EMBL; AK157917; BAE34262.1; -; mRNA.
DR   EMBL; AK158118; BAE34364.1; -; mRNA.
DR   EMBL; AK158405; BAE34491.1; -; mRNA.
DR   EMBL; AK160729; BAE35974.1; -; mRNA.
DR   EMBL; AK162392; BAE36889.1; -; mRNA.
DR   EMBL; BC145907; AAI45908.1; -; mRNA.
DR   EMBL; BC145909; AAI45910.1; -; mRNA.
DR   CCDS; CCDS28105.1; -.
DR   PIR; S49581; S49581.
DR   RefSeq; NP_001288282.1; NM_001301353.1.
DR   RefSeq; NP_001288283.1; NM_001301354.1.
DR   RefSeq; NP_031496.2; NM_007470.4.
DR   AlphaFoldDB; P51910; -.
DR   SMR; P51910; -.
DR   STRING; 10090.ENSMUSP00000119827; -.
DR   GlyConnect; 2131; 1 N-Linked glycan (1 site).
DR   GlyGen; P51910; 2 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P51910; -.
DR   PhosphoSitePlus; P51910; -.
DR   CPTAC; non-CPTAC-3382; -.
DR   MaxQB; P51910; -.
DR   PaxDb; P51910; -.
DR   PeptideAtlas; P51910; -.
DR   PRIDE; P51910; -.
DR   ProteomicsDB; 296381; -.
DR   Antibodypedia; 19470; 378 antibodies from 37 providers.
DR   DNASU; 11815; -.
DR   Ensembl; ENSMUST00000115230; ENSMUSP00000110885; ENSMUSG00000022548.
DR   Ensembl; ENSMUST00000130560; ENSMUSP00000119827; ENSMUSG00000022548.
DR   GeneID; 11815; -.
DR   KEGG; mmu:11815; -.
DR   UCSC; uc007yxf.2; mouse.
DR   CTD; 347; -.
DR   MGI; MGI:88056; Apod.
DR   VEuPathDB; HostDB:ENSMUSG00000022548; -.
DR   eggNOG; KOG4824; Eukaryota.
DR   GeneTree; ENSGT00510000046981; -.
DR   HOGENOM; CLU_068449_2_1_1; -.
DR   InParanoid; P51910; -.
DR   OMA; YSCTTIV; -.
DR   OrthoDB; 1631943at2759; -.
DR   PhylomeDB; P51910; -.
DR   TreeFam; TF324836; -.
DR   Reactome; R-MMU-804914; Transport of fatty acids.
DR   BioGRID-ORCS; 11815; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Apod; mouse.
DR   PRO; PR:P51910; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P51910; protein.
DR   Bgee; ENSMUSG00000022548; Expressed in vestibular membrane of cochlear duct and 229 other tissues.
DR   Genevisible; P51910; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0022626; C:cytosolic ribosome; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR   GO; GO:0007568; P:aging; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0060588; P:negative regulation of lipoprotein lipid oxidation; IMP:UniProtKB.
DR   GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; ISS:UniProtKB.
DR   GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:2000098; P:negative regulation of smooth muscle cell-matrix adhesion; ISS:UniProtKB.
DR   GO; GO:2000405; P:negative regulation of T cell migration; ISS:UniProtKB.
DR   GO; GO:0014012; P:peripheral nervous system axon regeneration; ISS:UniProtKB.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:UniProtKB.
DR   GO; GO:0042246; P:tissue regeneration; ISS:UniProtKB.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR026222; ApoD_vertbrte.
DR   InterPro; IPR002969; ApolipopD.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR022271; Lipocalin_ApoD.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   Pfam; PF08212; Lipocalin_2; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PRINTS; PR02058; APODVERTBRTE.
DR   PRINTS; PR01219; APOLIPOPROTD.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Lipid-binding; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..189
FT                   /note="Apolipoprotein D"
FT                   /id="PRO_0000017874"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P05090"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..185
FT                   /evidence="ECO:0000250"
FT   VARIANT         146
FT                   /note="V -> F (in strain: Swiss Webster)"
SQ   SEQUENCE   189 AA;  21530 MW;  C10109F1D56D69A0 CRC64;
     MVTMLMFLAT LAGLFTTAKG QNFHLGKCPS PPVQENFDVK KYLGRWYEIE KIPASFEKGN
     CIQANYSLME NGNIEVLNKE LSPDGTMNQV KGEAKQSNVS EPAKLEVQFF PLMPPAPYWI
     LATDYENYAL VYSCTTFFWL FHVDFVWILG RNPYLPPETI TYLKDILTSN GIDIEKMTTT
     DQANCPDFL
 
 
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