SCLT1_MOUSE
ID SCLT1_MOUSE Reviewed; 688 AA.
AC G5E861; Q6PAJ0; Q9CSV4; Q9CUR9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Sodium channel and clathrin linker 1;
DE AltName: Full=Sodium channel-associated protein 1;
GN Name=Sclt1; Synonyms=Sap1;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-359 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
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: Adapter protein that links SCN10A to clathrin. Regulates
CC SCN10A channel activity, possibly by promoting channel internalization
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SCN10A and clathrin. Identified in a complex
CC containing SCN10A, clathrin and SCLT1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Note=Localizes to the
CC distal appendage region of the centriole, which anchors the mother
CC centriole to the plasma membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=G5E861-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G5E861-2; Sequence=VSP_047144, VSP_047145;
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DR EMBL; AC102795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466530; EDL35173.1; -; Genomic_DNA.
DR EMBL; BC043136; AAH43136.1; -; mRNA.
DR EMBL; BC060271; AAH60271.1; -; mRNA.
DR EMBL; AK011907; BAB27908.1; -; mRNA.
DR EMBL; AK014777; BAB29547.1; -; mRNA.
DR CCDS; CCDS38425.1; -. [G5E861-1]
DR RefSeq; NP_001074880.1; NM_001081411.1. [G5E861-1]
DR AlphaFoldDB; G5E861; -.
DR SMR; G5E861; -.
DR BioGRID; 211987; 1.
DR STRING; 10090.ENSMUSP00000026866; -.
DR iPTMnet; G5E861; -.
DR PhosphoSitePlus; G5E861; -.
DR EPD; G5E861; -.
DR MaxQB; G5E861; -.
DR PaxDb; G5E861; -.
DR PRIDE; G5E861; -.
DR ProteomicsDB; 255490; -. [G5E861-1]
DR ProteomicsDB; 255491; -. [G5E861-2]
DR Antibodypedia; 45370; 147 antibodies from 22 providers.
DR DNASU; 67161; -.
DR Ensembl; ENSMUST00000026866; ENSMUSP00000026866; ENSMUSG00000059834. [G5E861-1]
DR Ensembl; ENSMUST00000148769; ENSMUSP00000123392; ENSMUSG00000059834. [G5E861-2]
DR GeneID; 67161; -.
DR KEGG; mmu:67161; -.
DR UCSC; uc008pcn.1; mouse. [G5E861-1]
DR CTD; 132320; -.
DR MGI; MGI:1914411; Sclt1.
DR VEuPathDB; HostDB:ENSMUSG00000059834; -.
DR eggNOG; ENOG502QS6B; Eukaryota.
DR GeneTree; ENSGT00730000111168; -.
DR HOGENOM; CLU_025503_0_0_1; -.
DR InParanoid; G5E861; -.
DR OMA; SRSQEMI; -.
DR OrthoDB; 729964at2759; -.
DR PhylomeDB; G5E861; -.
DR TreeFam; TF331372; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 67161; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Sclt1; mouse.
DR PRO; PR:G5E861; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; G5E861; protein.
DR Bgee; ENSMUSG00000059834; Expressed in spermatid and 224 other tissues.
DR ExpressionAtlas; G5E861; baseline and differential.
DR Genevisible; G5E861; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0097539; C:ciliary transition fiber; ISO:MGI.
DR GO; GO:0071439; C:clathrin complex; ISO:MGI.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISO:MGI.
DR InterPro; IPR038911; SCLT1.
DR PANTHER; PTHR35970; PTHR35970; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96NL6"
FT CHAIN 2..688
FT /note="Sodium channel and clathrin linker 1"
FT /id="PRO_0000422822"
FT COILED 59..108
FT /evidence="ECO:0000255"
FT COILED 152..673
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96NL6"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 350
FT /note="I -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047144"
FT VAR_SEQ 351..688
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047145"
SQ SEQUENCE 688 AA; 80492 MW; B5EB86C7B9F4A94C CRC64;
MATEIDLLRD QKDKLNDILR QHQIEHIFRD PTMQNSMSKG GRGDTLVDSI NEQSSLPPLI
AEYEKHLEEL NRQLTYYQKH MGEMKLQLET VITENERLHS KLKDAVEKQL EALPFGTGIG
NDICADDETV RILQEQLQLA NQEKTWALEL WQTASQELQS VQKLYQEHMT EAQIHEFENR
KQKDQLNNFQ QLTKKLHVAN ENIEMTNHHF LKTVTEQNME IEKLRKHLRQ ARLDLRVAVS
KVEELTKVTE GLQEQMLKKE EDIMSAQGKE EASDRRVQQL QSSIKQLESR LCVAIEEADV
LKTGKSNLEK QIKELQAKCS ESENEKYEAI SRARDSMQLL EEANIKQNQI LLEEKQKEVD
REKMKKTMSQ LIQDAAIKAR KEVESTKKQY EILISQLKEE LSTLQMDCDE KQGQIDRAIR
GKRAVEEELE KIYREGKQDE SDYRKLEEMH QRCLAAERSK DDLQLRLKSA ENRIKQLEIN
SSEEMSRSHE MIQKLQTVLE SERENCGFVS EQRLKLQQEN EQLQKETEDL RKVALEAQKK
AKLKVSTMEH QFSIKEHGFE VQLREMEDSN RNSIVELRHL LAAQQKTANR WKEETKKLTE
SAEMRISSLK SELSRQKLHT QELLSQLEMA NEKVAENEKL ILEHQEKANR LQRRLSQAEE
RAASASQQLS VITVQRRKAA SMMNLENI
