SCLT1_RAT
ID SCLT1_RAT Reviewed; 688 AA.
AC Q8CJ99; Q8CJ83; Q8CJ84; Q8CJ98;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Sodium channel and clathrin linker 1;
DE AltName: Full=Clathrin-associated protein 1A;
DE Short=CAP-1A;
DE AltName: Full=Sodium channel Nav1.8-binding protein;
DE AltName: Full=Sodium channel-associated protein 1;
GN Name=Sclt1; Synonyms=Sap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP CLATHRIN AND SCN10A, IDENTIFICATION IN A COMPLEX WITH CLATHRIN AND SCN10A,
RP AND TISSUE SPECIFICITY.
RX PubMed=15797711; DOI=10.1016/j.mcn.2004.11.007;
RA Liu C., Cummins T.R., Tyrrell L., Black J.A., Waxman S.G., Dib-Hajj S.D.;
RT "CAP-1A is a novel linker that binds clathrin and the voltage-gated sodium
RT channel Na(v)1.8.";
RL Mol. Cell. Neurosci. 28:636-649(2005).
CC -!- FUNCTION: Adapter protein that links SCN10A to clathrin. Regulates
CC SCN10A channel activity, possibly by promoting channel internalization.
CC {ECO:0000269|PubMed:15797711}.
CC -!- SUBUNIT: Interacts with SCN10A and clathrin. Identified in a complex
CC containing SCN10A, clathrin and SCLT1. {ECO:0000269|PubMed:15797711}.
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; Synonyms=SAP1A;
CC IsoId=Q8CJ99-1; Sequence=Displayed;
CC Name=2; Synonyms=SAP1B;
CC IsoId=Q8CJ99-2; Sequence=VSP_030908;
CC -!- TISSUE SPECIFICITY: Detected in small neurons in dorsal root ganglia.
CC Detected in C-type fibers of sciatic nerve (at protein level).
CC {ECO:0000269|PubMed:15797711}.
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DR EMBL; AF421190; AAN32724.1; -; mRNA.
DR EMBL; AF421191; AAN32725.1; -; mRNA.
DR EMBL; AF427094; AAN63528.1; -; mRNA.
DR EMBL; AF427095; AAN63529.1; -; mRNA.
DR RefSeq; NP_714962.1; NM_153740.1. [Q8CJ99-1]
DR AlphaFoldDB; Q8CJ99; -.
DR SMR; Q8CJ99; -.
DR CORUM; Q8CJ99; -.
DR STRING; 10116.ENSRNOP00000019256; -.
DR CarbonylDB; Q8CJ99; -.
DR iPTMnet; Q8CJ99; -.
DR PhosphoSitePlus; Q8CJ99; -.
DR PaxDb; Q8CJ99; -.
DR PRIDE; Q8CJ99; -.
DR Ensembl; ENSRNOT00000019256; ENSRNOP00000019256; ENSRNOG00000014139. [Q8CJ99-1]
DR GeneID; 266809; -.
DR KEGG; rno:266809; -.
DR UCSC; RGD:628721; rat. [Q8CJ99-1]
DR CTD; 132320; -.
DR RGD; 628721; Sclt1.
DR eggNOG; ENOG502QS6B; Eukaryota.
DR GeneTree; ENSGT00730000111168; -.
DR HOGENOM; CLU_025503_0_0_1; -.
DR InParanoid; Q8CJ99; -.
DR OMA; SRSQEMI; -.
DR OrthoDB; 729964at2759; -.
DR PhylomeDB; Q8CJ99; -.
DR TreeFam; TF331372; -.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR PRO; PR:Q8CJ99; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014139; Expressed in testis and 19 other tissues.
DR Genevisible; Q8CJ99; RN.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0097539; C:ciliary transition fiber; ISO:RGD.
DR GO; GO:0071439; C:clathrin complex; IDA:RGD.
DR GO; GO:0030276; F:clathrin binding; IDA:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:RGD.
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_0000317128"
FT COILED 59..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:0000250|UniProtKB:G5E861"
FT VAR_SEQ 1..35
FT /note="MATEIDLLRDQNVKLNDILRQHQIEHIFRDPAMQN -> MIFLGSIKSNIFS
FT ETQLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15797711"
FT /id="VSP_030908"
SQ SEQUENCE 688 AA; 80329 MW; BEB5621DEEAF7967 CRC64;
MATEIDLLRD QNVKLNDILR QHQIEHIFRD PAMQNSMSKG GRGDTLTNSV NDQSALPPLI
AEYEKHLEEL NRQLTYYQKH MGEMKLQLET VITENERLHS KLKDAVEKQL EALPFGTGIG
NDICADDETV RNLQEQLQIA NQEKNWAVQL WQTASQELES VQKLYQEHMT EAQIHVFENR
KQKDQLNNFQ QLTKKLHVAN ENIEMTNHHF LKTVTEQNME IEKLRKQLRQ AKLDLRVAVT
KVEELTKVTE GLQEQMLKKE EDIMSAQGKE EASDRRVQQL QSSIKQLESR LCIAIQEANV
LKTGKTQLEK QIKELQAKCS ESENEKYEAI SRARDSMQLL EEANIKQNQI LLEEKQKEVE
REKMKKTISH LIQDAAIKAR KEVESTKKQY EVLILQLKEE LSALQMDCDE KQGQIDRAIR
GKRAVEEELE KIYREGKQDE GDYRKLEEMH QRCLAAERSK DDLQLRLKTA ENRIKQLEIN
SSEEISRSHE MIQKLQTVLE SERENCGFVS EQRLKLQQEN EQLQKETEDL RKVALEAQKK
AKLKVSTMEH QFSIKEHGFE VQLREMEDSN RNSIVELRHL LAAQQKTANR WKEETKKLTE
SAEMRISSLK SELSRQKLHT QELLSQLEMA NEKVAENEKL ILEHQEKANR LQRRLSQAEE
RAASASQQLS VITVQRRKAA SMMNLENI
