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PANX3_MOUSE
ID   PANX3_MOUSE             Reviewed;         392 AA.
AC   Q8CEG0; Q8CB28;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Pannexin-3;
GN   Name=Panx3;
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=Embryonic head;
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   STRAIN=C3H/He; TISSUE=Osteoblast;
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]
RP   GLYCOSYLATION AT ASN-71, AND MUTAGENESIS OF ASN-71.
RX   PubMed=17925379; DOI=10.1242/jcs.009514;
RA   Penuela S., Bhalla R., Gong X.Q., Cowan K.N., Celetti S.J., Cowan B.J.,
RA   Bai D., Shao Q., Laird D.W.;
RT   "Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct
RT   characteristics from the connexin family of gap junction proteins.";
RL   J. Cell Sci. 120:3772-3783(2007).
CC   -!- FUNCTION: Structural component of the gap junctions and the
CC       hemichannels.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC       junction.
CC   -!- TISSUE SPECIFICITY: Expressed in skin, cartilage, heart, lung, liver,
CC       spleen, thymus and kidney. Not expressed in brain.
CC   -!- PTM: N-glycosylation may play a role in cell surface targeting.
CC       {ECO:0000269|PubMed:17925379}.
CC   -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00351}.
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DR   EMBL; AK028288; BAC25860.1; -; mRNA.
DR   EMBL; AK036933; BAC29644.1; -; mRNA.
DR   EMBL; BC052822; AAH52822.1; -; mRNA.
DR   CCDS; CCDS22984.1; -.
DR   RefSeq; NP_766042.2; NM_172454.2.
DR   AlphaFoldDB; Q8CEG0; -.
DR   SMR; Q8CEG0; -.
DR   STRING; 10090.ENSMUSP00000011262; -.
DR   GlyGen; Q8CEG0; 1 site.
DR   iPTMnet; Q8CEG0; -.
DR   PhosphoSitePlus; Q8CEG0; -.
DR   EPD; Q8CEG0; -.
DR   PaxDb; Q8CEG0; -.
DR   PRIDE; Q8CEG0; -.
DR   Antibodypedia; 53990; 94 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000011262; ENSMUSP00000011262; ENSMUSG00000011118.
DR   GeneID; 208098; -.
DR   KEGG; mmu:208098; -.
DR   UCSC; uc009ovi.1; mouse.
DR   CTD; 116337; -.
DR   MGI; MGI:1918881; Panx3.
DR   VEuPathDB; HostDB:ENSMUSG00000011118; -.
DR   eggNOG; ENOG502QRDI; Eukaryota.
DR   GeneTree; ENSGT00940000153972; -.
DR   HOGENOM; CLU_050054_1_0_1; -.
DR   InParanoid; Q8CEG0; -.
DR   OMA; SDPYVFW; -.
DR   OrthoDB; 623546at2759; -.
DR   PhylomeDB; Q8CEG0; -.
DR   TreeFam; TF333142; -.
DR   BioGRID-ORCS; 208098; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Panx3; mouse.
DR   PRO; PR:Q8CEG0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8CEG0; protein.
DR   Bgee; ENSMUSG00000011118; Expressed in vault of skull and 58 other tissues.
DR   ExpressionAtlas; Q8CEG0; baseline and differential.
DR   Genevisible; Q8CEG0; MM.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR   GO; GO:0022829; F:wide pore channel activity; IBA:GO_Central.
DR   GO; GO:0006812; P:cation transport; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR   GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:InterPro.
DR   InterPro; IPR000990; Innexin.
DR   InterPro; IPR039099; Pannexin.
DR   PANTHER; PTHR15759; PTHR15759; 1.
DR   Pfam; PF00876; Innexin; 1.
DR   PROSITE; PS51013; PANNEXIN; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Gap junction; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..392
FT                   /note="Pannexin-3"
FT                   /id="PRO_0000208492"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        61..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        135..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        237..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        289..392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17925379"
FT   MUTAGEN         71
FT                   /note="N->Q: Impairs glycosylation."
FT                   /evidence="ECO:0000269|PubMed:17925379"
FT   CONFLICT        192
FT                   /note="L -> V (in Ref. 1; BAC29644)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  44928 MW;  F78A6C1CD7B4C8A1 CRC64;
     MSLAHTAAEY MLSDALLPDR RGSRLKGLRL ELPLDKMVKF ITVGFPLLLM SLAFAQEFSS
     GSPISCFSPS NFSVRQAAYV DSSCWDSLAH HTQDKAGQYK VKSLWPHKAL PYSLLALAVA
     MYLPVLLWQY VAVPSLSSDL LFIISELDKS YNRSIRLVQH MLQIRQSSSD PHVFWDELEK
     ARKERYFEFP LLERYLECKQ RSHWLVATYL LRNALLLLFT SATYLYLGQF HLDVFFQDEF
     NCFIKTGLLH DETHVPELIT CRLTSLSVFQ IVSVSSAAIY TILVPVIIYN LTRLCRWDKG
     LLSIYEMLPA FDLLSRKMLG CPINDLNVIL LFLRANISEL ISFSWLSVLS VLKDTTTQKH
     NIDTVVDFMT FVAGLEPSKP KHLTQHTYDE HA
 
 
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