CAMLG_MOUSE
ID CAMLG_MOUSE Reviewed; 294 AA.
AC P49070; Q99JU5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Guided entry of tail-anchored proteins factor CAMLG {ECO:0000305};
DE AltName: Full=Calcium signal-modulating cyclophilin ligand {ECO:0000250|UniProtKB:P49069};
GN Name=Camlg {ECO:0000250|UniProtKB:P49069};
GN Synonyms=Caml {ECO:0000312|MGI:MGI:104728},
GN Get2 {ECO:0000250|UniProtKB:P49069};
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 [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX PubMed=7590290; DOI=10.1016/0378-1119(95)00393-k;
RA Kim H.S., Morales V.M., Dass C., Encinas J., Teitell M., Blumberg R.S.;
RT "Cloning of the gene encoding the mouse homologue of the human calcium
RT signal-modulating ligand.";
RL Gene 163:323-324(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE OF 1-55.
RA Morales V.M., Snapper S.B., Blumberg R.S.;
RT "Sequence of the promoter region of the mouse CAMLG gene.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
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).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22351938; DOI=10.4049/jimmunol.1101641;
RA Zane N.A., Gundelach J.H., Lindquist L.D., Bram R.J.;
RT "Essential role for CAML in follicular B cell survival and homeostasis.";
RL J. Immunol. 188:3009-3018(2012).
RN [6]
RP MUTAGENESIS OF ARG-202 AND LYS-207.
RX PubMed=32910895; DOI=10.1016/j.molcel.2020.08.012;
RA McDowell M.A., Heimes M., Fiorentino F., Mehmood S., Farkas A.,
RA Coy-Vergara J., Wu D., Bolla J.R., Schmid V., Heinze R., Wild K.,
RA Flemming D., Pfeffer S., Schwappach B., Robinson C.V., Sinning I.;
RT "Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET
RT Insertase Complex.";
RL Mol. Cell 80:72-86(2020).
CC -!- FUNCTION: Required for the post-translational delivery of tail-anchored
CC (TA) proteins to the endoplasmic reticulum (By similarity). Together
CC with GET1/WRB, acts as a membrane receptor for soluble GET3/TRC40,
CC which recognizes and selectively binds the transmembrane domain of TA
CC proteins in the cytosol (By similarity). Required for the stability of
CC GET1 (By similarity). Stimulates calcium signaling in T cells through
CC its involvement in elevation of intracellular calcium (By similarity).
CC Essential for the survival of peripheral follicular B cells
CC (PubMed:22351938). {ECO:0000250|UniProtKB:P49069,
CC ECO:0000269|PubMed:22351938}.
CC -!- SUBUNIT: Component of the Golgi to ER traffic (GET) complex, which is
CC composed of GET1/WRB, CAMLG/GET2 and GET3/TRC40 (By similarity). Within
CC the complex, GET1 and CAMLG form a heterotetramer which is stabilized
CC by phosphatidylinositol binding and which binds to the GET3 homodimer
CC (By similarity). Interacts (via C-terminus) with GET1 (By similarity).
CC Interacts (via N-terminus) with GET3 (By similarity). GET3 shows a
CC higher affinity for CAMLG than for GET1 (By similarity). Interacts (via
CC N-terminus) with TNFRSF13B/TACI (via C-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:P49069, ECO:0000250|UniProtKB:Q6DGG9}.
CC -!- INTERACTION:
CC P49070; E9PZQ0: Ryr1; NbExp=3; IntAct=EBI-309114, EBI-642079;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P49069}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in B cells results in
CC significant reduction in the number of mature follicular B cells with
CC normal cellular proliferation but increased cellular turnover.
CC {ECO:0000269|PubMed:22351938}.
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DR EMBL; U21960; AAA87004.1; -; mRNA.
DR EMBL; BC005688; AAH05688.1; -; mRNA.
DR EMBL; AF078112; AAC33940.1; -; Genomic_DNA.
DR CCDS; CCDS26551.1; -.
DR RefSeq; NP_031622.2; NM_007596.2.
DR AlphaFoldDB; P49070; -.
DR SMR; P49070; -.
DR CORUM; P49070; -.
DR IntAct; P49070; 4.
DR MINT; P49070; -.
DR STRING; 10090.ENSMUSP00000021963; -.
DR iPTMnet; P49070; -.
DR PhosphoSitePlus; P49070; -.
DR SwissPalm; P49070; -.
DR EPD; P49070; -.
DR jPOST; P49070; -.
DR MaxQB; P49070; -.
DR PaxDb; P49070; -.
DR PeptideAtlas; P49070; -.
DR PRIDE; P49070; -.
DR ProteomicsDB; 265516; -.
DR Antibodypedia; 26345; 299 antibodies from 30 providers.
DR DNASU; 12328; -.
DR Ensembl; ENSMUST00000021963; ENSMUSP00000021963; ENSMUSG00000021501.
DR GeneID; 12328; -.
DR KEGG; mmu:12328; -.
DR UCSC; uc007qrv.1; mouse.
DR CTD; 12328; -.
DR MGI; MGI:104728; Caml.
DR VEuPathDB; HostDB:ENSMUSG00000021501; -.
DR eggNOG; ENOG502QVCE; Eukaryota.
DR GeneTree; ENSGT00390000015996; -.
DR HOGENOM; CLU_081881_0_0_1; -.
DR InParanoid; P49070; -.
DR OMA; GNAVEEF; -.
DR OrthoDB; 1203862at2759; -.
DR PhylomeDB; P49070; -.
DR TreeFam; TF331902; -.
DR BioGRID-ORCS; 12328; 24 hits in 75 CRISPR screens.
DR PRO; PR:P49070; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P49070; protein.
DR Bgee; ENSMUSG00000021501; Expressed in medial ganglionic eminence and 253 other tissues.
DR Genevisible; P49070; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0043529; C:GET complex; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; IMP:MGI.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR016719; CAMLG.
DR PANTHER; PTHR15026; PTHR15026; 1.
DR Pfam; PF14963; Get2_like; 1.
DR PIRSF; PIRSF018259; CAML; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..294
FT /note="Guided entry of tail-anchored proteins factor CAMLG"
FT /id="PRO_0000089292"
FT TOPO_DOM 1..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT TRANSMEM 188..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..210
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT TRANSMEM 268..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..294
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT DISULFID 206..282
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT MUTAGEN 202
FT /note="R->A: Impaired tail-anchored protein insertion and a
FT shift from GET1-CAMLG heterotetramerization to formation of
FT heterodimers but does not affect recruitment of GET3 to the
FT endoplasmic reticulum; when associated with A-207."
FT /evidence="ECO:0000269|PubMed:32910895"
FT MUTAGEN 207
FT /note="K->A: Impaired tail-anchored protein insertion and a
FT shift from GET1-CAMLG heterotetramerization to formation of
FT heterodimers but does not affect recruitment of GET3 to the
FT endoplasmic reticulum; when associated with A-202."
FT /evidence="ECO:0000269|PubMed:32910895"
FT CONFLICT 254
FT /note="V -> A (in Ref. 1; AAA87004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 32542 MW; D21AC54BC9F609E5 CRC64;
MEPVPAATDG GERPATPSGL SASQRRAELR RRKLLMNSEQ RINRIMGFHR PGSGSEEENQ
TKSKPQDSDK LNSLSIPSVS KRVVLGDSVD GGGADQLGGV AEVRGTQLGD KLDSFIKAPE
CSSKDGAELR QRTRGDLTAD PAQRASHHGL EQYLSRFEEA MKLRKQLISE KPSQEDGSTA
EEFDSFRIFR LVGCALLALG VRAFVCKYLS IFAPFLTLQL AYMGLYKYFP KGEKKVKTTV
LTAALLLSGI PAEVINRSMD TYSKMGEVFT DLCVYFFTFI FCHELLDYWG PEVP
