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PADC1_MOUSE
ID   PADC1_MOUSE             Reviewed;         188 AA.
AC   Q9D9N8;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Protease-associated domain-containing protein 1 {ECO:0000305};
DE   AltName: Full=Protease-associated domain-containing protein of 21 kDa;
DE   Flags: Precursor;
GN   Name=Pradc1 {ECO:0000312|MGI:MGI:1920577};
GN   Synonyms=Pap21 {ECO:0000303|PubMed:31689374};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
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).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP   FEEDING.
RX   PubMed=31689374; DOI=10.1096/fj.201901279r;
RA   Rodriguez S., Stewart A.N., Lei X., Cao X., Little H.C., Fong V.,
RA   Sarver D.C., Wong G.W.;
RT   "PRADC1: a novel metabolic-responsive secretory protein that modulates
RT   physical activity and adiposity.";
RL   FASEB J. 33:14748-14759(2019).
CC   -!- FUNCTION: Plays a role in the modulation of physical activity and
CC       adiposity. {ECO:0000269|PubMed:31689374}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9BSG0}.
CC   -!- TISSUE SPECIFICITY: Expressed in metabolically active tissues such as
CC       liver, muscle, adipose, and heart and different brain regions like
CC       cortex and hypothalamus, expression is acutely regulated by the
CC       nutritional state. {ECO:0000269|PubMed:31689374}.
CC   -!- INDUCTION: Expression in metabolically active tissues is significantly
CC       suppressed by refeeding. {ECO:0000269|PubMed:31689374}.
CC   -!- PTM: N-glycosylated; required for efficient secretion.
CC       {ECO:0000250|UniProtKB:Q9BSG0}.
CC   -!- DISRUPTION PHENOTYPE: Mutants born at the expected Mendelian ratio, and
CC       they appear normal with no gross developmental abnormalities
CC       (PubMed:31689374). Knockout female mice fed with high fat diet have
CC       reduced weight gain by elevating physical activity and energy
CC       expenditure (PubMed:31689374). {ECO:0000269|PubMed:31689374}.
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DR   EMBL; AK006658; BAB24693.1; -; mRNA.
DR   CCDS; CCDS51828.1; -.
DR   RefSeq; NP_001156899.1; NM_001163427.1.
DR   RefSeq; NP_082781.1; NM_028505.2.
DR   RefSeq; XP_011239788.1; XM_011241486.1.
DR   AlphaFoldDB; Q9D9N8; -.
DR   SMR; Q9D9N8; -.
DR   STRING; 10090.ENSMUSP00000032080; -.
DR   GlyGen; Q9D9N8; 2 sites.
DR   PhosphoSitePlus; Q9D9N8; -.
DR   EPD; Q9D9N8; -.
DR   PaxDb; Q9D9N8; -.
DR   PRIDE; Q9D9N8; -.
DR   ProteomicsDB; 287934; -.
DR   Antibodypedia; 31326; 16 antibodies from 8 providers.
DR   Ensembl; ENSMUST00000032080; ENSMUSP00000032080; ENSMUSG00000030008.
DR   GeneID; 73327; -.
DR   KEGG; mmu:73327; -.
DR   UCSC; uc009cps.2; mouse.
DR   CTD; 84279; -.
DR   MGI; MGI:1920577; Pradc1.
DR   VEuPathDB; HostDB:ENSMUSG00000030008; -.
DR   eggNOG; KOG3920; Eukaryota.
DR   GeneTree; ENSGT00390000009837; -.
DR   HOGENOM; CLU_084006_2_0_1; -.
DR   InParanoid; Q9D9N8; -.
DR   OMA; KINHPPW; -.
DR   OrthoDB; 1302890at2759; -.
DR   PhylomeDB; Q9D9N8; -.
DR   TreeFam; TF335463; -.
DR   BioGRID-ORCS; 73327; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q9D9N8; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9D9N8; protein.
DR   Bgee; ENSMUSG00000030008; Expressed in primary oocyte and 248 other tissues.
DR   ExpressionAtlas; Q9D9N8; baseline and differential.
DR   Genevisible; Q9D9N8; MM.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   CDD; cd02127; PA_hPAP21_like; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR042773; PADC1.
DR   InterPro; IPR037323; PRADC1-like_PA.
DR   PANTHER; PTHR22702; PTHR22702; 1.
DR   Pfam; PF02225; PA; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..188
FT                   /note="Protease-associated domain-containing protein 1"
FT                   /id="PRO_0000022002"
FT   DOMAIN          83..163
FT                   /note="PA"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   188 AA;  21085 MW;  AC61BEEBB0159D40 CRC64;
     MSRGAAGWCC LVLWLPTCVA AHGLRIHDYL YFQVLSPGDI RYIFTATPAK DFGGIFHTRY
     EQIHLVPAEP PEACGELSNG FFIQDQIALV ERGGCSFLSK TRVVQEHGGR AVIISDNAVD
     NDSFYVEMIQ DSTQRTADIP ALFLLGRDGY MIRRSLEQHG LPWAIISIPV NVTSIPTFEL
     LQPPWTFW
 
 
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