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CDHR3_MOUSE
ID   CDHR3_MOUSE             Reviewed;         831 AA.
AC   Q8BL00; B2RSL6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Cadherin-related family member 3;
DE   AltName: Full=Cadherin-like protein 28;
DE   Flags: Precursor;
GN   Name=Cdhr3; Synonyms=Cdh28;
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=Corpus striatum, and Hippocampus;
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).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6ZTQ4};
CC       Single-pass type I membrane protein {ECO:0000250}.
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DR   EMBL; AK047666; BAC33118.1; -; mRNA.
DR   EMBL; AK049806; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC138911; AAI38912.1; -; mRNA.
DR   CCDS; CCDS36430.1; -.
DR   RefSeq; NP_001019649.1; NM_001024478.1.
DR   RefSeq; XP_006515253.1; XM_006515190.3.
DR   AlphaFoldDB; Q8BL00; -.
DR   SMR; Q8BL00; -.
DR   STRING; 10090.ENSMUSP00000093449; -.
DR   GlyGen; Q8BL00; 3 sites.
DR   iPTMnet; Q8BL00; -.
DR   PhosphoSitePlus; Q8BL00; -.
DR   PaxDb; Q8BL00; -.
DR   PRIDE; Q8BL00; -.
DR   ProteomicsDB; 281516; -.
DR   Antibodypedia; 2413; 65 antibodies from 16 providers.
DR   DNASU; 68764; -.
DR   Ensembl; ENSMUST00000095774; ENSMUSP00000093449; ENSMUSG00000035860.
DR   GeneID; 68764; -.
DR   KEGG; mmu:68764; -.
DR   UCSC; uc007nij.1; mouse.
DR   CTD; 222256; -.
DR   MGI; MGI:1916014; Cdhr3.
DR   VEuPathDB; HostDB:ENSMUSG00000035860; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   eggNOG; KOG4289; Eukaryota.
DR   GeneTree; ENSGT00940000161245; -.
DR   HOGENOM; CLU_017741_0_0_1; -.
DR   InParanoid; Q8BL00; -.
DR   OMA; AGHKSFH; -.
DR   OrthoDB; 592155at2759; -.
DR   PhylomeDB; Q8BL00; -.
DR   TreeFam; TF336601; -.
DR   BioGRID-ORCS; 68764; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q8BL00; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8BL00; protein.
DR   Bgee; ENSMUSG00000035860; Expressed in olfactory epithelium and 39 other tissues.
DR   Genevisible; Q8BL00; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   Pfam; PF00028; Cadherin; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; SSF49313; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..831
FT                   /note="Cadherin-related family member 3"
FT                   /id="PRO_0000305904"
FT   TOPO_DOM        20..711
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        712..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        733..831
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..132
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          136..236
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          237..344
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          346..466
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          462..570
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          567..693
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          743..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   831 AA;  92084 MW;  989B3DAFCEAAFCAB CRC64;
     MQGAVIVLVL FGITSGGEAL HLLHLPATSN VAENAPPATL VHKFSVNLSV SLSPVIPGFP
     LVVNPRPFTE AFRVNRLSAT NFEVVTTGKE QLDFERGPKA FDLQIYVKDD VGVTDVQVLT
     VQVTDVNEPP QFQGILAQGL NLYVIERTNP GFIYQVEAFD PEDTSRSIPL GYFLISPSKN
     FRMSANGTLF STTELDFEAG HKSFNLLVGV RDSGNLEAST ALQVTIVNIN DETPRFTSPR
     RVYSVPEEVP LGTMVANITA MDPDDEGFPG RLLYSITTTS SYFMVDQLTG TIQVARRLDR
     DAGELRQNPI ISLEVRVRDR PSGGQENRMQ ITFIVEDIND NPATCRKLTF SIMLPERTAN
     GTLLLDLNKF CFDDDSEAPN NKFNFTTPSG AGSSRRFSQH PAGSGRIVLT GDLDYENPSN
     LAVGNVYNVM IQVQDAAPPY YKKSIYISIL TRPENEFPLI FERPSYVFDV PERRPARTQI
     GQVRATDADF PRTPVVYSVS RGGSSLQYPN IFWINPKTGE LQLITQADHE TTSVYILTVE
     ATNGEDRSSV TVTVNILGEN DEKPVCTPNF YFMAIPVDLK VGTNIQNFKL TCTDLDSSPS
     SFRYSIGSGN INNHFTFSPN AGSNITRLLL ASRFDYSSLD TVWDYQLLVH ITDDNLLSGS
     TKAKALVETG TVTLSVKVIP HPTTTITTPR PRITYQIRRE NVYSTSAWYV PFIVTLGSIL
     LLGLLGSLMV LLSKAVYRHC SSTTRRDRKP LTKKRDTKRM NREAMVESIQ MNSVFDGEAV
     DPVTGEIYEF NSKTGARRWK GPLTQLPNWP EPSTQHRGTA GEAPVPKHTG R
 
 
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