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APCD1_MOUSE
ID   APCD1_MOUSE             Reviewed;         514 AA.
AC   Q3U128; B2RUN4; Q3TA99;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Protein APCDD1;
DE   AltName: Full=Adenomatosis polyposis coli down-regulated 1 protein homolog;
DE   Flags: Precursor;
GN   Name=Apcdd1 {ECO:0000312|MGI:MGI:3513977};
GN   Synonyms=Drapc1 {ECO:0000303|PubMed:15465500};
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] {ECO:0000312|EMBL:BAE33672.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD {ECO:0000312|EMBL:BAE33672.1};
RC   TISSUE=Spleen {ECO:0000312|EMBL:BAE33672.1};
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   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   [3] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15465500; DOI=10.1016/j.modgep.2004.03.006;
RA   Jukkola T., Sinjushina N., Partanen J.;
RT   "Drapc1 expression during mouse embryonic development.";
RL   Gene Expr. Patterns 4:755-762(2004).
CC   -!- FUNCTION: Negative regulator of the Wnt signaling pathway. Inhibits Wnt
CC       signaling in a cell-autonomous manner and functions upstream of beta-
CC       catenin. May act via its interaction with Wnt and LRP proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with LRP5 and WNT3A (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during early development of the
CC       extraembryonic structures, nervous system, vascular system and inner
CC       ear. Also expressed in mesenchyme of various parts of the embryo and in
CC       adult hair follicles. {ECO:0000269|PubMed:15465500}.
CC   -!- INDUCTION: APCDD1 is transcriptionally regulated by the CTNNB1/TF7L2
CC       complex. {ECO:0000250|UniProtKB:Q8J025}.
CC   -!- PTM: N-Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the APCDD1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE42770.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK156319; BAE33672.1; -; mRNA.
DR   EMBL; AK172004; BAE42770.1; ALT_SEQ; mRNA.
DR   EMBL; BC141269; AAI41270.1; -; mRNA.
DR   EMBL; BC141270; AAI41271.1; -; mRNA.
DR   CCDS; CCDS37843.1; -.
DR   RefSeq; NP_573500.2; NM_133237.3.
DR   AlphaFoldDB; Q3U128; -.
DR   STRING; 10090.ENSMUSP00000094302; -.
DR   GlyGen; Q3U128; 3 sites.
DR   iPTMnet; Q3U128; -.
DR   PhosphoSitePlus; Q3U128; -.
DR   EPD; Q3U128; -.
DR   MaxQB; Q3U128; -.
DR   PaxDb; Q3U128; -.
DR   PRIDE; Q3U128; -.
DR   ProteomicsDB; 281826; -.
DR   Antibodypedia; 2521; 175 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000096554; ENSMUSP00000094302; ENSMUSG00000071847.
DR   Ensembl; ENSMUST00000163716; ENSMUSP00000125868; ENSMUSG00000071847.
DR   Ensembl; ENSMUST00000236135; ENSMUSP00000157539; ENSMUSG00000071847.
DR   GeneID; 494504; -.
DR   KEGG; mmu:494504; -.
DR   UCSC; uc008fdl.1; mouse.
DR   CTD; 147495; -.
DR   MGI; MGI:3513977; Apcdd1.
DR   VEuPathDB; HostDB:ENSMUSG00000071847; -.
DR   eggNOG; ENOG502QQ0C; Eukaryota.
DR   GeneTree; ENSGT00640000091492; -.
DR   HOGENOM; CLU_035648_0_0_1; -.
DR   InParanoid; Q3U128; -.
DR   OMA; GRHTWPL; -.
DR   OrthoDB; 613671at2759; -.
DR   PhylomeDB; Q3U128; -.
DR   TreeFam; TF329491; -.
DR   BioGRID-ORCS; 494504; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; Apcdd1; mouse.
DR   PRO; PR:Q3U128; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q3U128; protein.
DR   Bgee; ENSMUSG00000071847; Expressed in brain blood vessel and 290 other tissues.
DR   ExpressionAtlas; Q3U128; baseline and differential.
DR   Genevisible; Q3U128; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR   GO; GO:0043615; P:astrocyte cell migration; IDA:MGI.
DR   GO; GO:0001942; P:hair follicle development; ISO:MGI.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IMP:CACAO.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR042425; APCDD1.
DR   InterPro; IPR029405; APCDD1_dom.
DR   PANTHER; PTHR31021; PTHR31021; 1.
DR   Pfam; PF14921; APCDDC; 2.
DR   SMART; SM01352; APCDDC; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..514
FT                   /note="Protein APCDD1"
FT                   /id="PRO_0000227521"
FT   TOPO_DOM        27..492
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        514
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          437..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   514 AA;  58638 MW;  0657A8DF94C5F65E CRC64;
     MSRVRRLLLG YLFPALLLHG LGEGSALLHP DSRSHPRSLE KSAWRAFKES QCHHMLKHLH
     NGARITVQMP PTIEGHWVST GCEVRSGPEF MTRSYRFYNN NTFKAYQFYY GSNRCTNPTY
     TLIIRGKIRL RQASWIIRGG TEADYQLHGV QVICHTEAVA EQLSRLVNRT CPGFLAPGGP
     WVQDVAYDLW QEESNHECTK AVNFAMHELQ LIRVEKQYPH HSLDHLVEEL FLGDIHTDAT
     QRVFYRPSSY QPPLQNAKNH NHACIACRII FRSDEHHPPI LPPKADLTIG LHGEWVSQRC
     EVRPEVLFLT RHFIFHDNNN TWEGHYYHYS DPVCKHPTFT IYARGRYSRG VLSSKVMGGT
     EFVFKVNHMK VTPMDAATAS LLNVFSGNEC GAEGSWQVGI QQDVTHTNGC VALGIKLPHT
     EYEIFKMEQD TRGRYLLFNG QRPSDGSSPD RPEKRATSYQ MPLVQCASSS PRAEELLEDS
     QGHLYGRAAG RTAGSLLLPA FVSLWTLPHW RILR
 
 
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