CLVS1_MOUSE
ID CLVS1_MOUSE Reviewed; 354 AA.
AC Q9D4C9; Q3UWV3; Q497H3; Q8BJE8; Q8BXX0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Clavesin-1;
DE AltName: Full=Retinaldehyde-binding protein 1-like 1;
GN Name=Clvs1; Synonyms=Rlbp1l1;
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; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Egg, Eye, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
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=3;
CC Name=1;
CC IsoId=Q9D4C9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D4C9-2; Sequence=VSP_027331;
CC Name=3;
CC IsoId=Q9D4C9-3; Sequence=VSP_027330;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22811.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK016622; BAB30342.1; -; mRNA.
DR EMBL; AK043072; BAC31451.1; -; mRNA.
DR EMBL; AK084350; BAC39166.1; -; mRNA.
DR EMBL; AK136083; BAE22811.1; ALT_INIT; mRNA.
DR EMBL; AL671970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062923; AAH62923.1; -; mRNA.
DR EMBL; BC100556; AAI00557.1; -; mRNA.
DR CCDS; CCDS17957.1; -. [Q9D4C9-1]
DR RefSeq; NP_083216.1; NM_028940.2. [Q9D4C9-1]
DR RefSeq; XP_011248427.1; XM_011250125.2.
DR AlphaFoldDB; Q9D4C9; -.
DR SMR; Q9D4C9; -.
DR STRING; 10090.ENSMUSP00000035649; -.
DR iPTMnet; Q9D4C9; -.
DR PhosphoSitePlus; Q9D4C9; -.
DR SwissPalm; Q9D4C9; -.
DR MaxQB; Q9D4C9; -.
DR PaxDb; Q9D4C9; -.
DR PeptideAtlas; Q9D4C9; -.
DR PRIDE; Q9D4C9; -.
DR ProteomicsDB; 283863; -. [Q9D4C9-1]
DR ProteomicsDB; 283864; -. [Q9D4C9-2]
DR ProteomicsDB; 283865; -. [Q9D4C9-3]
DR Antibodypedia; 24702; 98 antibodies from 18 providers.
DR Ensembl; ENSMUST00000038841; ENSMUSP00000035649; ENSMUSG00000041216. [Q9D4C9-1]
DR Ensembl; ENSMUST00000108348; ENSMUSP00000103985; ENSMUSG00000041216. [Q9D4C9-1]
DR GeneID; 74438; -.
DR KEGG; mmu:74438; -.
DR UCSC; uc008ryc.2; mouse. [Q9D4C9-2]
DR UCSC; uc008rye.2; mouse. [Q9D4C9-1]
DR CTD; 157807; -.
DR MGI; MGI:1921688; Clvs1.
DR VEuPathDB; HostDB:ENSMUSG00000041216; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000159947; -.
DR HOGENOM; CLU_046597_1_3_1; -.
DR InParanoid; Q9D4C9; -.
DR OMA; DSAKMTH; -.
DR OrthoDB; 1182715at2759; -.
DR PhylomeDB; Q9D4C9; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR BioGRID-ORCS; 74438; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Clvs1; mouse.
DR PRO; PR:Q9D4C9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D4C9; protein.
DR Bgee; ENSMUSG00000041216; Expressed in facial nucleus and 178 other tissues.
DR Genevisible; Q9D4C9; 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; IPR028634; Clavesin-1.
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:SF72; PTHR10174:SF72; 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..354
FT /note="Clavesin-1"
FT /id="PRO_0000297656"
FT DOMAIN 118..279
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 317..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..279
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027330"
FT VAR_SEQ 153..354
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027331"
FT CONFLICT 307
FT /note="H -> Q (in Ref. 1; BAE22811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40613 MW; 894F8BB1EE4E8AEF CRC64;
MGPVSVLPSP QSLSTWEGDL AKMTHLQAGL SPDTIEKARL ELNENPDILH QDIQQVRDMI
ITRPDIGFLR TDDAFILRFL RARKFHQADA FRLLAQYFQY RQLNLDMFKN FKADDPGIKR
ALIDGFPGVL ENRDHYGRKI LLLFAANWDQ SRNSFTDILR AILLSLEVLI EDPELQINGF
ILIIDWSNFS FKQASKLTPS ILKLAIEGLQ DSFPARFGGV HFVNQPWYIH ALYTLIKPFL
KDKTRKRIFL HGNNLNSLHQ LIHPEFLPSE FGGTLPPYDM GTWARTLLGP DYSDENDYTH
TSYNAMHVKH TCSNLERECS PKPMKRSQSV VEAGTLKHEE KGENENTQPL LALD
