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CLVS2_MOUSE
ID   CLVS2_MOUSE             Reviewed;         327 AA.
AC   Q8BG92; Q8BKA5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Clavesin-2;
DE   AltName: Full=Retinaldehyde-binding protein 1-like 2;
GN   Name=Clvs2; Synonyms=Rlbp1l2;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Eye, Hippocampus, Spinal cord, and Stomach;
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J; 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]
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: Required for normal morphology of late endosomes and/or
CC       lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate
CC       (PtdIns(3,5)P2) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Early
CC       endosome membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BG92-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG92-2; Sequence=VSP_027326, VSP_027327;
CC   -!- DOMAIN: The CRAL-TRIO domain is required for targeting to the membrane
CC       and for binding PtdIns(3,5)P2. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC       localization. {ECO:0000250}.
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DR   EMBL; AK039308; BAC30312.1; -; mRNA.
DR   EMBL; AK049896; BAC33976.1; -; mRNA.
DR   EMBL; AK053797; BAC35529.1; -; mRNA.
DR   EMBL; AK139409; BAE23998.1; -; mRNA.
DR   EMBL; AK169009; BAE40806.1; -; mRNA.
DR   EMBL; BC058539; AAH58539.1; -; mRNA.
DR   CCDS; CCDS23770.1; -. [Q8BG92-1]
DR   RefSeq; NP_780657.1; NM_175448.3. [Q8BG92-1]
DR   RefSeq; XP_017169371.1; XM_017313882.1.
DR   AlphaFoldDB; Q8BG92; -.
DR   SMR; Q8BG92; -.
DR   STRING; 10090.ENSMUSP00000019920; -.
DR   iPTMnet; Q8BG92; -.
DR   PhosphoSitePlus; Q8BG92; -.
DR   MaxQB; Q8BG92; -.
DR   PaxDb; Q8BG92; -.
DR   PeptideAtlas; Q8BG92; -.
DR   PRIDE; Q8BG92; -.
DR   ProteomicsDB; 281691; -. [Q8BG92-1]
DR   ProteomicsDB; 281692; -. [Q8BG92-2]
DR   Antibodypedia; 46590; 90 antibodies from 19 providers.
DR   DNASU; 215890; -.
DR   Ensembl; ENSMUST00000019920; ENSMUSP00000019920; ENSMUSG00000019785. [Q8BG92-1]
DR   Ensembl; ENSMUST00000160299; ENSMUSP00000125100; ENSMUSG00000019785. [Q8BG92-2]
DR   GeneID; 215890; -.
DR   KEGG; mmu:215890; -.
DR   UCSC; uc007eue.1; mouse. [Q8BG92-1]
DR   UCSC; uc007euf.1; mouse. [Q8BG92-2]
DR   CTD; 134829; -.
DR   MGI; MGI:2443223; Clvs2.
DR   VEuPathDB; HostDB:ENSMUSG00000019785; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   GeneTree; ENSGT00940000157632; -.
DR   HOGENOM; CLU_046597_1_3_1; -.
DR   InParanoid; Q8BG92; -.
DR   OMA; TQNYYPE; -.
DR   OrthoDB; 872816at2759; -.
DR   PhylomeDB; Q8BG92; -.
DR   Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR   BioGRID-ORCS; 215890; 2 hits in 71 CRISPR screens.
DR   PRO; PR:Q8BG92; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8BG92; protein.
DR   Bgee; ENSMUSG00000019785; Expressed in secondary oocyte and 94 other tissues.
DR   ExpressionAtlas; Q8BG92; baseline and differential.
DR   Genevisible; Q8BG92; MM.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; -; 1.
DR   InterPro; IPR028636; Clavesin-2.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   PANTHER; PTHR10174:SF73; PTHR10174:SF73; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF46938; SSF46938; 1.
DR   SUPFAM; SSF52087; SSF52087; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW   Lipid-binding; Membrane; Reference proteome.
FT   CHAIN           1..327
FT                   /note="Clavesin-2"
FT                   /id="PRO_0000297653"
FT   DOMAIN          96..257
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          289..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         189..227
FT                   /note="DSFPARFGGIHFVNQPWYIHALYTVIRPFLKEKTRKRIF -> VRVHHCYCF
FT                   FVSCMVLALFVMYWVSYEIVKTPNQKFIDF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027326"
FT   VAR_SEQ         228..327
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027327"
SQ   SEQUENCE   327 AA;  37954 MW;  B3F9F8D35E025B77 CRC64;
     MTHLQAGLSP ETLEKARLEL NENPDTLHQD IQEVRDMVIT RPDIGFLRTD DAFILRFLRA
     RKFHHFEAFR LLAQYFEYRQ QNLDMFKSFK ATDPGIKQAL KDGFPGGLAN LDHYGRKILV
     LFAANWDQSR YTLVDILRAI LLSLEAMIED PELQVNGFVL IIDWSNFTFK QASKLTPNML
     RLAIEGLQDS FPARFGGIHF VNQPWYIHAL YTVIRPFLKE KTRKRIFLHG NNLNSLHQLI
     HPEILPSEFG GMLPPYDMGT WARTLLDHEY DDDSEYNVDS YNMPVKDVDK ELSPKSMKRS
     QSVVDPTALK RMDKSEEENM QPLLALD
 
 
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