CAMLG_RAT
ID CAMLG_RAT Reviewed; 295 AA.
AC Q6DGG9; F7FMD6; Q9ERK1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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:0000312|RGD:69297};
GN Synonyms=Caml {ECO:0000303|PubMed:11762198},
GN Get2 {ECO:0000250|UniProtKB:P49069};
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 {ECO:0000312|EMBL:AAH76377.1};
RN [1] {ECO:0000312|EMBL:AAG21394.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11762198; DOI=10.3109/10425170109080777;
RA Lee S.J., Drabik K., Benveniste E.N.;
RT "Cloning of rat calcium-modulating cyclophilin ligand.";
RL DNA Seq. 12:209-213(2001).
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000312|EMBL:EDL93961.1}
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 [4] {ECO:0000312|EMBL:AAH76377.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH76377.1};
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 [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN GET COMPLEX, AND INTERACTION WITH GET1 AND
RP GET3.
RX PubMed=23041287; DOI=10.1016/j.molcel.2012.08.028;
RA Yamamoto Y., Sakisaka T.;
RT "Molecular machinery for insertion of tail-anchored membrane proteins into
RT the endoplasmic reticulum membrane in mammalian cells.";
RL Mol. Cell 48:387-397(2012).
CC -!- FUNCTION: Required for the post-translational delivery of tail-anchored
CC (TA) proteins to the endoplasmic reticulum (PubMed:23041287). 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 (PubMed:23041287). Required for the stability
CC of GET1 (By similarity). Stimulates calcium signaling in T cells
CC through its involvement in elevation of intracellular calcium (By
CC similarity). Essential for the survival of peripheral follicular B
CC cells (By similarity). {ECO:0000250|UniProtKB:P49069,
CC ECO:0000250|UniProtKB:P49070, ECO:0000269|PubMed:23041287}.
CC -!- SUBUNIT: Component of the Golgi to ER traffic (GET) complex, which is
CC composed of GET1/WRB, CAMLG/GET2 and GET3/TRC40 (PubMed:23041287).
CC Within the complex, GET1 and CAMLG form a heterotetramer which is
CC stabilized by phosphatidylinositol binding and which binds to the GET3
CC homodimer (By similarity). Interacts (via C-terminus) with GET1
CC (PubMed:23041287). Interacts (via N-terminus) with GET3
CC (PubMed:23041287). GET3 shows a higher affinity for CAMLG than for GET1
CC (By similarity). Interacts (via N-terminus) with TNFRSF13B/TACI (via C-
CC terminus) (By similarity). {ECO:0000250|UniProtKB:P49069,
CC ECO:0000269|PubMed:23041287}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P49069}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the central nervous system, expressed in
CC astrocytes, microglia and neurons (at protein level).
CC {ECO:0000269|PubMed:11762198}.
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DR EMBL; AF302085; AAG21394.1; -; mRNA.
DR EMBL; AC139608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474032; EDL93961.1; -; Genomic_DNA.
DR EMBL; BC076377; AAH76377.1; -; mRNA.
DR RefSeq; NP_445786.1; NM_053334.1.
DR RefSeq; XP_006253720.1; XM_006253658.3.
DR AlphaFoldDB; Q6DGG9; -.
DR SMR; Q6DGG9; -.
DR IntAct; Q6DGG9; 1.
DR STRING; 10116.ENSRNOP00000033945; -.
DR PhosphoSitePlus; Q6DGG9; -.
DR jPOST; Q6DGG9; -.
DR PaxDb; Q6DGG9; -.
DR PRIDE; Q6DGG9; -.
DR GeneID; 81715; -.
DR KEGG; rno:81715; -.
DR CTD; 819; -.
DR RGD; 69297; Camlg.
DR VEuPathDB; HostDB:ENSRNOG00000021911; -.
DR eggNOG; ENOG502QVCE; Eukaryota.
DR HOGENOM; CLU_081881_0_0_1; -.
DR OMA; GNAVEEF; -.
DR OrthoDB; 1203862at2759; -.
DR PhylomeDB; Q6DGG9; -.
DR TreeFam; TF331902; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0043529; C:GET complex; IPI:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; ISO:RGD.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA: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..295
FT /note="Guided entry of tail-anchored proteins factor CAMLG"
FT /id="PRO_0000452582"
FT TOPO_DOM 1..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT TRANSMEM 189..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..208
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..295
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..148
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 207..283
FT /evidence="ECO:0000250|UniProtKB:P49069"
FT CONFLICT 16
FT /note="T -> A (in Ref. 1; AAG21394)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="Missing (in Ref. 1; AAG21394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32790 MW; FA840DD127E3B1EF CRC64;
MEPMPSATDG GDRSATPSGL SASQRRAELR RRKLLMNSEQ RINRIMGFHR PGSGAEEENQ
TKSKPLDSDI LNPLGVPSVS KRVVLGDSVD GGVTDYQPSG GADIRGAQLG DKLDSFIKAP
ECSSKDGVEL RQRNRGDLTA DSAPRGSHHG LEQYLSRFEE AMKLRKQLIS EKPSQEDGRT
TEEFDSFRIF RLVGCALLAL VVRAFVCKYL SIFAPFLTLQ LAYMGLYKYF PKGEKKVKTT
VLTAALLLSG IPAEVINRSM DTYSKMGEVF TDLCVYFFTF IFCHEVLEYW GPEVP
