CASP_CAEEL
ID CASP_CAEEL Reviewed; 621 AA.
AC Q8IA98; Q9BL01;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein CASP;
GN Name=ceh-44; ORFNames=Y54F10AM.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION, AND ALTERNATIVE SPLICING.
RX PubMed=11902672;
RA Buerglin T.R., Cassata G.;
RT "Loss and gain of domains during evolution of cut superclass homeobox
RT genes.";
RL Int. J. Dev. Biol. 46:115-123(2002).
RN [3]
RP IDENTIFICATION, AND ALTERNATIVE SPLICING.
RX PubMed=12429822; DOI=10.1091/mbc.e02-06-0349;
RA Gillingham A.K., Pfeifer A.C., Munro S.;
RT "CASP, the alternatively spliced product of the gene encoding the CCAAT-
RT displacement protein transcription factor, is a Golgi membrane protein
RT related to giantin.";
RL Mol. Biol. Cell 13:3761-3774(2002).
CC -!- FUNCTION: May be involved in intra-Golgi retrograde transport.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b;
CC IsoId=Q8IA98-1; Sequence=Displayed;
CC Name=c;
CC IsoId=Q8IA98-2; Sequence=VSP_017009;
CC Name=a;
CC IsoId=Q9BL02-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the CASP family. {ECO:0000305}.
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DR EMBL; FO081806; CCD73823.1; -; Genomic_DNA.
DR EMBL; FO081806; CCD73824.1; -; Genomic_DNA.
DR RefSeq; NP_497575.2; NM_065174.5. [Q8IA98-2]
DR RefSeq; NP_497577.2; NM_065176.5. [Q8IA98-1]
DR AlphaFoldDB; Q8IA98; -.
DR SMR; Q8IA98; -.
DR BioGRID; 40620; 3.
DR EPD; Q8IA98; -.
DR PeptideAtlas; Q8IA98; -.
DR EnsemblMetazoa; Y54F10AM.4b.1; Y54F10AM.4b.1; WBGene00000464. [Q8IA98-2]
DR EnsemblMetazoa; Y54F10AM.4c.1; Y54F10AM.4c.1; WBGene00000464. [Q8IA98-1]
DR GeneID; 175372; -.
DR KEGG; cel:CELE_Y54F10AM.4; -.
DR UCSC; Y54F10AM.4c; c. elegans. [Q8IA98-1]
DR CTD; 175372; -.
DR WormBase; Y54F10AM.4b; CE32987; WBGene00000464; ceh-44. [Q8IA98-2]
DR WormBase; Y54F10AM.4c; CE32988; WBGene00000464; ceh-44. [Q8IA98-1]
DR HOGENOM; CLU_441623_0_0_1; -.
DR OMA; DNWEAKE; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000464; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q8IA98; baseline and differential.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR012955; CASP_C.
DR Pfam; PF08172; CASP_C; 2.
PE 3: Inferred from homology;
KW Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..621
FT /note="Protein CASP"
FT /id="PRO_0000071793"
FT TOPO_DOM 1..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..621
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 101..445
FT /evidence="ECO:0000255"
FT COILED 473..525
FT /evidence="ECO:0000255"
FT VAR_SEQ 541..543
FT /note="DFR -> E (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_017009"
SQ SEQUENCE 621 AA; 70952 MW; F75BF5E889583BCB CRC64;
MEIVSRAWES VDWDRIQTRV EAEVTALGQR QDDSEIRKTR LVEESNAYRG RTNKDSRKVA
IPLIKAFQSE FDGLLARSTA AENALIDICK SIVSLPDPKS LLKGAEAWKN DAEKTQKAVE
EREELKRQLI KVNNELEDLR GKDVKVRKLK DKLAKLESEQ DIFIENAVNE VEKKAEQELN
DRLTELIAEK EKMKEQNEIL EKNMDSLESK NKDIQRKLEI AKQTVEQKDG LENEQLSIAM
KDLADAKHKI VFLEERVSQL ENEAEKVNES KKAGNIEDIA ALGSVLVQKD DVIQQLTNDI
KRHEASHVEE LAKWKLAVSA VEKKNKTLIG ELNELKNQLE SRNDYEAIKN ELRLLREIEF
GDSAEANAES IERLGETVET LDRLLAEKNR RLQNENASLR VANDGFKGRN EEQEAELTVL
KEKSERNDRL IAQLEADLAS AVQDIGIPER MGTNEMLKDA PAPTISDASL VPILTSQRNR
LHERVTSLEE AISLEKTKQL SVQNEIERVR EENIRLCERI RFLQSPGGQQ QANVEAGLGN
DFRNGNRNKK VSLHDKTTLN MGRAILATPK SRTVFFSYLL ILHALIMLVL YKFAFDQSVV
RDAETECEYK FHQHMLDNHK Q