ID   CAMLG_HUMAN             Reviewed;         296 AA.
AC   P49069; A1L3Y3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   28-JAN-2026, entry version 185.
DE   RecName: Full=Guided entry of tail-anchored proteins factor CAMLG {ECO:0000305};
DE   AltName: Full=Calcium signal-modulating cyclophilin ligand {ECO:0000312|HGNC:HGNC:1471};
GN   Name=CAMLG {ECO:0000312|HGNC:HGNC:1471};
GN   Synonyms=CAML {ECO:0000303|PubMed:24392163,
GN   ECO:0000312|HGNC:HGNC:1471}, GET2 {ECO:0000312|HGNC:HGNC:1471};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=7522304; DOI=10.1038/371355a0;
RA   Bram R.J., Crabtree G.R.;
RT   "Calcium signalling in T cells stimulated by a cyclophilin B-binding
RT   protein.";
RL   Nature 371:355-358(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-296.
RC   TISSUE=Colon adenocarcinoma;
RA   Morales V.M., Blumberg R.S.;
RT   "An immature transcript of the CAMLG gene.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH TNFRSF13B.
RX   PubMed=9311921; DOI=10.1126/science.278.5335.138;
RA   von Buelow G.-U., Bram R.J.;
RT   "NF-AT activation induced by a CAML-interacting member of the tumor
RT   necrosis factor receptor superfamily.";
RL   Science 278:138-141(1997).
RN   [7]
RP   INTERACTION WITH HHV-8 PROTEIN K7 (MICROBIAL INFECTION).
RX   PubMed=12388711; DOI=10.1128/jvi.76.22.11491-11504.2002;
RA   Feng P., Park J., Lee B.S., Lee S.H., Bram R.J., Jung J.U.;
RT   "Kaposi's sarcoma-associated herpesvirus mitochondrial K7 protein targets a
RT   cellular calcium-modulating cyclophilin ligand to modulate intracellular
RT   calcium concentration and inhibit apoptosis.";
RL   J. Virol. 76:11491-11504(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   FUNCTION, IDENTIFICATION IN GET COMPLEX, SUBCELLULAR LOCATION,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF 32-ARG--LYS-35.
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).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH GET1 AND GET3.
RX   PubMed=24392163; DOI=10.1371/journal.pone.0085033;
RA   Vilardi F., Stephan M., Clancy A., Janshoff A., Schwappach B.;
RT   "WRB and CAML are necessary and sufficient to mediate tail-anchored protein
RT   targeting to the ER membrane.";
RL   PLoS ONE 9:e85033-e85033(2014).
RN   [13]
RP   FUNCTION.
RX   PubMed=27226539; DOI=10.1074/jbc.m115.707752;
RA   Colombo S.F., Cardani S., Maroli A., Vitiello A., Soffientini P.,
RA   Crespi A., Bram R.F., Benfante R., Borgese N.;
RT   "Tail-anchored protein insertion in mammals: function and reciprocal
RT   interactions of the two subunits of the TRC40 receptor.";
RL   J. Biol. Chem. 291:15292-15306(2016).
RN   [14]
RP   INTERACTION WITH GET1, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=31417168; DOI=10.1038/s41598-019-48363-2;
RA   Carvalho H.J.F., Del Bondio A., Maltecca F., Colombo S.F., Borgese N.;
RT   "The WRB Subunit of the Get3 Receptor is Required for the Correct
RT   Integration of its Partner CAML into the ER.";
RL   Sci. Rep. 9:11887-11887(2019).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH GET1.
RX   PubMed=32187542; DOI=10.1016/j.celrep.2020.02.084;
RA   Inglis A.J., Page K.R., Guna A., Voorhees R.M.;
RT   "Differential Modes of Orphan Subunit Recognition for the WRB/CAML
RT   Complex.";
RL   Cell Rep. 30:3691-3698(2020).
RN   [16]
RP   INVOLVEMENT IN CDG2Z.
RX   PubMed=35262690; DOI=10.1093/hmg/ddac055;
RA   Wilson M.P., Durin Z., Unal O., Ng B.G., Marrecau T., Keldermans L.,
RA   Souche E., Rymen D., Guenduez M., Koese G., Sturiale L., Garozzo D.,
RA   Freeze H.H., Jaeken J., Foulquier F., Matthijs G.;
RT   "CAMLG-CDG: a novel congenital disorder of glycosylation linked to
RT   defective membrane trafficking.";
RL   Hum. Mol. Genet. 31:2571-2581(2022).
RN   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF THE GET COMPLEX, AND
RP   DISULFIDE BOND.
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 (PubMed:23041287,
CC       PubMed:24392163, PubMed:27226539). Together with GET1/WRB, acts as a
CC       membrane receptor for soluble GET3/TRC40, which recognizes and
CC       selectively binds the transmembrane domain of TA proteins in the
CC       cytosol (PubMed:23041287, PubMed:24392163, PubMed:27226539). Required
CC       for the stability of GET1 (PubMed:32187542). Stimulates calcium
CC       signaling in T cells through its involvement in elevation of
CC       intracellular calcium (PubMed:7522304). Essential for the survival of
CC       peripheral follicular B cells (By similarity).
CC       {ECO:0000250|UniProtKB:P49070, ECO:0000269|PubMed:23041287,
CC       ECO:0000269|PubMed:24392163, ECO:0000269|PubMed:27226539,
CC       ECO:0000269|PubMed:32187542, ECO:0000269|PubMed:7522304}.
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       PubMed:24392163, PubMed:32910895). Within the complex, GET1 and CAMLG
CC       form a heterotetramer which is stabilized by phosphatidylinositol
CC       binding and which binds to the GET3 homodimer (PubMed:32910895).
CC       Interacts (via C-terminus) with GET1 (PubMed:24392163, PubMed:31417168,
CC       PubMed:32187542). Interacts (via N-terminus) with GET3 (By similarity).
CC       GET3 shows a higher affinity for CAMLG than for GET1 (PubMed:24392163).
CC       Interacts (via N-terminus) with TNFRSF13B/TACI (via C-terminus)
CC       (PubMed:9311921). {ECO:0000250|UniProtKB:Q6DGG9,
CC       ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:24392163,
CC       ECO:0000269|PubMed:31417168, ECO:0000269|PubMed:32187542,
CC       ECO:0000269|PubMed:32910895, ECO:0000269|PubMed:9311921}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 8/HHV-
CC       8 protein K7; this interaction modulates intracellular calcium
CC       concentration. {ECO:0000269|PubMed:12388711}.
CC   -!- INTERACTION:
CC       P49069; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-1748958, EBI-10827839;
CC       P49069; O95994: AGR2; NbExp=3; IntAct=EBI-1748958, EBI-712648;
CC       P49069; P00533: EGFR; NbExp=3; IntAct=EBI-1748958, EBI-297353;
CC       P49069; Q9HBU6: ETNK1; NbExp=3; IntAct=EBI-1748958, EBI-2834493;
CC       P49069; Q9Y624: F11R; NbExp=3; IntAct=EBI-1748958, EBI-742600;
CC       P49069; O00258: GET1; NbExp=3; IntAct=EBI-1748958, EBI-18908258;
CC       P49069; O43681: GET3; NbExp=8; IntAct=EBI-1748958, EBI-2515857;
CC       P49069; Q96GW1: HSP90B1; NbExp=3; IntAct=EBI-1748958, EBI-12885352;
CC       P49069; P46695: IER3; NbExp=2; IntAct=EBI-1748958, EBI-1748945;
CC       P49069; P16389: KCNA2; NbExp=4; IntAct=EBI-1748958, EBI-10210559;
CC       P49069; P16389-2: KCNA2; NbExp=3; IntAct=EBI-1748958, EBI-11987131;
CC       P49069; Q8WWG9: KCNE4; NbExp=3; IntAct=EBI-1748958, EBI-11750916;
CC       P49069; O43561-2: LAT; NbExp=3; IntAct=EBI-1748958, EBI-8070286;
CC       P49069; P80188: LCN2; NbExp=3; IntAct=EBI-1748958, EBI-11911016;
CC       P49069; Q9NX40: OCIAD1; NbExp=3; IntAct=EBI-1748958, EBI-2683029;
CC       P49069; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-1748958, EBI-740845;
CC       P49069; O00264: PGRMC1; NbExp=3; IntAct=EBI-1748958, EBI-1045534;
CC       P49069; P08F94: PKHD1; NbExp=3; IntAct=EBI-1748958, EBI-11693144;
CC       P49069; P04843: RPN1; NbExp=3; IntAct=EBI-1748958, EBI-355963;
CC       P49069; O95881: TXNDC12; NbExp=5; IntAct=EBI-1748958, EBI-2564581;
CC       P49069; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-1748958, EBI-11957238;
CC       P49069; Q7T6S2: NS7b; Xeno; NbExp=2; IntAct=EBI-1748958, EBI-25489089;
CC       P49069; E9PZ36: Pkhd1; Xeno; NbExp=4; IntAct=EBI-1748958, EBI-11693075;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:31417168}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in brain, testis and
CC       ovary.
CC   -!- DISEASE: Congenital disorder of glycosylation 2Z (CDG2Z) [MIM:620201]:
CC       A form of congenital disorder of glycosylation, a genetically
CC       heterogeneous group of multisystem disorders caused by a defect in
CC       glycoprotein biosynthesis and characterized by under-glycosylated serum
CC       glycoproteins. Congenital disorders of glycosylation result in a wide
CC       variety of clinical features, such as defects in the nervous system
CC       development, psychomotor retardation, dysmorphic features, hypotonia,
CC       coagulation disorders, and immunodeficiency. The broad spectrum of
CC       features reflects the critical role of N-glycoproteins during embryonic
CC       development, differentiation, and maintenance of cell functions. CDG2Z
CC       is an autosomal recessive form characterized by a predominantly
CC       neurological phenotype with psychomotor disability, hypotonia, epilepsy
CC       and structural brain abnormalities. Biochemically, CDG2Z is
CC       characterized by combined O- and N-linked glycosylation defects.
CC       {ECO:0000269|PubMed:35262690}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
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DR   EMBL; U18242; AAA59420.1; -; mRNA.
DR   EMBL; AK313156; BAG35974.1; -; mRNA.
DR   EMBL; CH471062; EAW62243.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW62244.1; -; Genomic_DNA.
DR   EMBL; BC130325; AAI30326.1; -; mRNA.
DR   EMBL; AF068179; AAC23596.1; -; mRNA.
DR   CCDS; CCDS4178.1; -.
DR   PIR; S47594; S47594.
DR   RefSeq; NP_001736.1; NM_001745.4.
DR   PDB; 6SO5; EM; 4.20 A; E/F=185-296.
DR   PDB; 8CR1; EM; 3.20 A; C/D=185-296.
DR   PDBsum; 6SO5; -.
DR   PDBsum; 8CR1; -.
DR   AlphaFoldDB; P49069; -.
DR   EMDB; EMD-10266; -.
DR   SMR; P49069; -.
DR   BioGRID; 107269; 156.
DR   ComplexPortal; CPX-6464; GET complex.
DR   CORUM; P49069; -.
DR   FunCoup; P49069; 2110.
DR   IntAct; P49069; 55.
DR   MINT; P49069; -.
DR   STRING; 9606.ENSP00000297156; -.
DR   DrugBank; DB12139; Alisporivir.
DR   DrugBank; DB00091; Cyclosporine.
DR   DrugBank; DB12451; SCY-635.
DR   DrugBank; DB11693; Voclosporin.
DR   TCDB; 3.A.19.1.1; the guided entry of tail anchored protein (get) family.
DR   GlyGen; P49069; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P49069; -.
DR   PhosphoSitePlus; P49069; -.
DR   SwissPalm; P49069; -.
DR   BioMuta; CAMLG; -.
DR   DMDM; 1345662; -.
DR   jPOST; P49069; -.
DR   MassIVE; P49069; -.
DR   PaxDb; 9606-ENSP00000297156; -.
DR   PeptideAtlas; P49069; -.
DR   ProteomicsDB; 55961; -.
DR   Pumba; P49069; -.
DR   Antibodypedia; 26345; 297 antibodies from 30 providers.
DR   DNASU; 819; -.
DR   Ensembl; ENST00000297156.4; ENSP00000297156.2; ENSG00000164615.7.
DR   GeneID; 819; -.
DR   KEGG; hsa:819; -.
DR   MANE-Select; ENST00000297156.4; ENSP00000297156.2; NM_001745.4; NP_001736.1.
DR   UCSC; uc003kzt.4; human.
DR   AGR; HGNC:1471; -.
DR   ClinPGx; PA26053; -.
DR   CTD; 819; -.
DR   DisGeNET; 819; -.
DR   GeneCards; CAMLG; -.
DR   HGNC; HGNC:1471; CAMLG.
DR   HPA; ENSG00000164615; Low tissue specificity.
DR   MalaCards; CAMLG; -.
DR   MIM; 601118; gene.
DR   MIM; 620201; phenotype.
DR   OpenTargets; ENSG00000164615; -.
DR   VEuPathDB; HostDB:ENSG00000164615; -.
DR   eggNOG; ENOG502QVCE; Eukaryota.
DR   GeneTree; ENSGT00390000015996; -.
DR   HOGENOM; CLU_081881_0_0_1; -.
DR   InParanoid; P49069; -.
DR   OMA; SFMKPPE; -.
DR   OrthoDB; 9895378at2759; -.
DR   PAN-GO; P49069; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; P49069; -.
DR   PathwayCommons; P49069; -.
DR   Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   SignaLink; P49069; -.
DR   Agora; ENSG00000164615; -.
DR   BioGRID-ORCS; 819; 256 hits in 1171 CRISPR screens.
DR   ChiTaRS; CAMLG; human.
DR   GeneWiki; CAMLG; -.
DR   GenomeRNAi; 819; -.
DR   Pharos; P49069; Tbio.
DR   PRO; PR:P49069; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P49069; protein.
DR   Bgee; ENSG00000164615; Expressed in secondary oocyte and 206 other cell types or tissues.
DR   ExpressionAtlas; P49069; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0043529; C:GET complex; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR   GO; GO:0006952; P:defense response; TAS:ProtInc.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR   GO; GO:0045048; P:protein insertion into ER membrane; NAS:ComplexPortal.
DR   GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR   GO; GO:0001881; P:receptor recycling; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; CALCIUM-SIGNAL MODULATING CYCLOPHILIN LIGAND CAML; 1.
DR   PANTHER; PTHR15026:SF0; GUIDED ENTRY OF TAIL-ANCHORED PROTEINS FACTOR CAMLG; 1.
DR   Pfam; PF14963; Get2_like; 1.
DR   PIRSF; PIRSF018259; CAML; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Congenital disorder of glycosylation; Disulfide bond;
KW   Endoplasmic reticulum; ER-Golgi transport; Host-virus interaction;
KW   Membrane; Phosphoprotein; Proteomics identification; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..296
FT                   /note="Guided entry of tail-anchored proteins factor CAMLG"
FT                   /id="PRO_0000089291"
FT   TOPO_DOM        1..189
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:31417168"
FT   TRANSMEM        190..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..212
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:31417168"
FT   TRANSMEM        213..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..269
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:31417168"
FT   TRANSMEM        270..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..296
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:31417168"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   DISULFID        208..284
FT                   /evidence="ECO:0000269|PubMed:32910895,
FT                   ECO:0007744|PDB:6SO5"
FT   VARIANT         78
FT                   /note="V -> I (in dbSNP:rs12657663)"
FT                   /id="VAR_024297"
FT   VARIANT         100
FT                   /note="G -> S (in dbSNP:rs11552197)"
FT                   /id="VAR_050710"
FT   MUTAGEN         32..35
FT                   /note="RRRK->EEEE: Abolishes binding to GET3."
FT                   /evidence="ECO:0000269|PubMed:23041287"
FT   HELIX           192..205
FT                   /evidence="ECO:0007829|PDB:8CR1"
FT   TURN            206..208
FT                   /evidence="ECO:0007829|PDB:8CR1"
FT   HELIX           215..230
FT                   /evidence="ECO:0007829|PDB:8CR1"
FT   HELIX           243..248
FT                   /evidence="ECO:0007829|PDB:8CR1"
FT   TURN            249..251
FT                   /evidence="ECO:0007829|PDB:8CR1"
FT   HELIX           254..290
FT                   /evidence="ECO:0007829|PDB:8CR1"
SQ   SEQUENCE   296 AA;  32953 MW;  22DCD8CF022FEF09 CRC64;
     MESMAVATDG GERPGVPAGS GLSASQRRAE LRRRKLLMNS EQRINRIMGF HRPGSGAEEE
     SQTKSKQQDS DKLNSLSVPS VSKRVVLGDS VSTGTTDQQG GVAEVKGTQL GDKLDSFIKP
     PECSSDVNLE LRQRNRGDLT ADSVQRGSRH GLEQYLSRFE EAMKLRKQLI SEKPSQEDGN
     TTEEFDSFRI FRLVGCALLA LGVRAFVCKY LSIFAPFLTL QLAYMGLYKY FPKSEKKIKT
     TVLTAALLLS GIPAEVINRS MDTYSKMGEV FTDLCVYFFT FIFCHELLDY WGSEVP
//