ID   CKLF6_PONAB             Reviewed;         183 AA.
AC   Q5RFC1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=CKLF-like MARVEL transmembrane domain-containing protein 6;
DE   AltName: Full=Chemokine-like factor superfamily member 6;
GN   Name=CMTM6; Synonyms=CKLFSF6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857239; CAH89536.1; -; mRNA.
DR   RefSeq; NP_001124667.1; NM_001131195.1.
DR   AlphaFoldDB; Q5RFC1; -.
DR   SMR; Q5RFC1; -.
DR   STRING; 9601.ENSPPYP00000015709; -.
DR   GeneID; 100171512; -.
DR   KEGG; pon:100171512; -.
DR   CTD; 54918; -.
DR   eggNOG; KOG4788; Eukaryota.
DR   InParanoid; Q5RFC1; -.
DR   OrthoDB; 1400503at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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_0000186109"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..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   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   MOD_RES         171
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX76"
SQ   SEQUENCE   183 AA;  20307 MW;  66195B411B4B02F5 CRC64;
     MENGAVYSPT TEEDPGPARG PRSGLAAYCF LGRLPLLRRV LKGLQLSLSL LAFICEEVVS
     QCTLCGGLYF FEFVSCSAFL LSLLILIVYC TPFYERVDTT KVKSSDFYIT LGTGCVFLLA
     SIIFVSTHDR TSAEIAAIVF GFIASFMFLL DFVTMLYEKR QESQLRKSEN TTRAEALTEP
     LNA