CKLF6_MOUSE
ID CKLF6_MOUSE Reviewed; 183 AA.
AC Q9CZ69; Q3U7C3; Q922J1;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=CKLF-like MARVEL transmembrane domain-containing protein 6;
DE AltName: Full=Chemokine-like factor superfamily member 6;
GN Name=Cmtm6 {ECO:0000312|MGI:MGI:2447165}; Synonyms=Cklfsf6;
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 TISSUE=Kidney;
RA Han W., Li T., Tan Y., Shi S., Ding P., Ma D.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Embryo, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- FUNCTION: Master regulator of recycling and plasma membrane expression
CC of PD-L1/CD274, an immune inhibitory ligand critical for immune
CC tolerance to self and antitumor immunity. Associates with both
CC constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where
CC it protects PD-L1/CD274 from being targeted for lysosomal degradation,
CC likely by preventing its ubiquitination. May stabilize PD-L1/CD274
CC expression on antigen presenting cells and potentiates inhibitory
CC signaling by PDCD1/CD279, its receptor on T-cells, ultimately
CC triggering T-cell anergy. {ECO:0000250|UniProtKB:Q9NX76}.
CC -!- SUBUNIT: Interacts with PD-L1/CD274 (via transmembrane domain); the
CC interaction is direct. Interacts with CMTM4. Interacts with CD58, ARG1,
CC ENO1 and TMPO. {ECO:0000250|UniProtKB:Q9NX76}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NX76};
CC Multi-pass membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9NX76}; Multi-pass membrane protein
CC {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9NX76}. Note=Co-localizes with PD-L1/CD274 in
CC the plasma membrane and in recycling endosomes.
CC {ECO:0000250|UniProtKB:Q9NX76}.
CC -!- SIMILARITY: Belongs to the chemokine-like factor family. {ECO:0000305}.
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DR EMBL; AY241868; AAP33490.1; -; mRNA.
DR EMBL; AK012941; BAB28562.1; -; mRNA.
DR EMBL; AK030885; BAC27172.1; -; mRNA.
DR EMBL; AK152448; BAE31227.1; -; mRNA.
DR EMBL; AK152723; BAE31446.1; -; mRNA.
DR EMBL; AK152817; BAE31520.1; -; mRNA.
DR EMBL; AK154481; BAE32617.1; -; mRNA.
DR EMBL; AK159735; BAE35329.1; -; mRNA.
DR EMBL; AK165948; BAE38480.1; -; mRNA.
DR EMBL; AK167499; BAE39575.1; -; mRNA.
DR EMBL; AK167854; BAE39872.1; -; mRNA.
DR EMBL; AK170905; BAE42106.1; -; mRNA.
DR EMBL; AK171394; BAE42431.1; -; mRNA.
DR EMBL; BC007194; AAH07194.1; -; mRNA.
DR EMBL; BC027248; AAH27248.1; -; mRNA.
DR CCDS; CCDS23596.1; -.
DR RefSeq; NP_080312.1; NM_026036.3.
DR AlphaFoldDB; Q9CZ69; -.
DR BioGRID; 212021; 1.
DR STRING; 10090.ENSMUSP00000035007; -.
DR iPTMnet; Q9CZ69; -.
DR PhosphoSitePlus; Q9CZ69; -.
DR EPD; Q9CZ69; -.
DR jPOST; Q9CZ69; -.
DR MaxQB; Q9CZ69; -.
DR PaxDb; Q9CZ69; -.
DR PRIDE; Q9CZ69; -.
DR ProteomicsDB; 279092; -.
DR Antibodypedia; 27750; 131 antibodies from 23 providers.
DR DNASU; 67213; -.
DR Ensembl; ENSMUST00000035007; ENSMUSP00000035007; ENSMUSG00000032434.
DR GeneID; 67213; -.
DR KEGG; mmu:67213; -.
DR UCSC; uc009ryb.1; mouse.
DR CTD; 54918; -.
DR MGI; MGI:2447165; Cmtm6.
DR VEuPathDB; HostDB:ENSMUSG00000032434; -.
DR eggNOG; KOG4788; Eukaryota.
DR GeneTree; ENSGT00940000157911; -.
DR HOGENOM; CLU_104458_1_0_1; -.
DR InParanoid; Q9CZ69; -.
DR OMA; VVMLCEK; -.
DR OrthoDB; 1400503at2759; -.
DR PhylomeDB; Q9CZ69; -.
DR TreeFam; TF317387; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 67213; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cmtm6; mouse.
DR PRO; PR:Q9CZ69; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CZ69; protein.
DR Bgee; ENSMUSG00000032434; Expressed in granulocyte and 249 other tissues.
DR Genevisible; Q9CZ69; MM.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR InterPro; IPR008253; Marvel.
DR Pfam; PF01284; MARVEL; 1.
DR PROSITE; PS51225; MARVEL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Endosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..183
FT /note="CKLF-like MARVEL transmembrane domain-containing
FT protein 6"
FT /id="PRO_0000186108"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..134
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 33..160
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX76"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX76"
FT CONFLICT 108..111
FT /note="YITL -> DAWV (in Ref. 3; AAH07194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 19824 MW; E5EFC4C4AA16720F CRC64;
MENGAVYSPT TEAAPGTGRG ARSGLAAYFV LGRLPWHRRI LKGLQLLLSL LAFICEEVVS
ECGLCGGLYF FEFVSCSAFL LSLLLLIVYC TPVHDRVDTG KVKSSDFYIT LGTGCVFLLA
SIIFVSTHSG TSAEIAAIVF GFLASSMFLL DFVVMLCEKL RESPLRKPEN NAKVEALTEP
LNA
