T4S20_MOUSE
ID T4S20_MOUSE Reviewed; 226 AA.
AC Q9CQY8; Q9D3Q0; Q9D3R0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transmembrane 4 L6 family member 20;
GN Name=Tm4sf20;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, Pancreas, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Polytopic transmembrane protein. Inhibits regulated
CC intramembrane proteolysis (RIP) of CREB3L1, inhibiting its activation
CC and the induction of collagen synthesis. In response to ceramide, which
CC alters TM4SF20 membrane topology, stimulates RIP activation of CREB3L1.
CC Ceramide reverses the direction through which transmembrane helices are
CC translocated into the endoplasmic reticulum membrane during translation
CC of TM4SF20, this mechanism is called 'regulated alternative
CC translocation' (RAT) and regulates the function of the transmembrane
CC protein. {ECO:0000250|UniProtKB:Q53R12}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q53R12}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q53R12}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q53R12}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q53R12}. Note=Ceramide alters the
CC direction through which transmembrane helices are translocated into the
CC endoplasmic reticulum membrane during translation of TM4SF20.
CC {ECO:0000250|UniProtKB:Q53R12}.
CC -!- DOMAIN: The first transmembrane helix plays a critical role for the
CC insertion orientation in the endoplasmic reticulum membrane.
CC {ECO:0000250|UniProtKB:Q53R12}.
CC -!- PTM: Glycosylated at Asn-132, Asn-148 and Asn-163 in presence of
CC ceramide which inverts the orientation of TM4SF20 in membranes exposing
CC these residues to the endoplasmic reticulum lumen.
CC {ECO:0000250|UniProtKB:Q53R12}.
CC -!- PTM: Cleaved by signal peptidase at Ser-14 but the peptide does not act
CC as a signal peptide. Cleavage is inhibited by ceramide which inverts
CC the orientation of TM4SF20 in membranes exposing the N-terminus to the
CC cytosol and not to the endoplasmic reticulum lumen.
CC {ECO:0000250|UniProtKB:Q53R12}.
CC -!- SIMILARITY: Belongs to the L6 tetraspanin family. {ECO:0000305}.
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DR EMBL; AK007532; BAB25093.1; -; mRNA.
DR EMBL; AK017154; BAB30618.1; -; mRNA.
DR EMBL; AK017195; BAB30629.1; -; mRNA.
DR EMBL; AK017209; BAB30635.1; -; mRNA.
DR EMBL; BC117736; AAI17737.1; -; mRNA.
DR CCDS; CCDS15099.1; -.
DR RefSeq; NP_079729.1; NM_025453.3.
DR AlphaFoldDB; Q9CQY8; -.
DR STRING; 10090.ENSMUSP00000027331; -.
DR PhosphoSitePlus; Q9CQY8; -.
DR MaxQB; Q9CQY8; -.
DR PaxDb; Q9CQY8; -.
DR PRIDE; Q9CQY8; -.
DR ProteomicsDB; 263238; -.
DR ABCD; Q9CQY8; 4 sequenced antibodies.
DR Antibodypedia; 47680; 65 antibodies from 15 providers.
DR DNASU; 66261; -.
DR Ensembl; ENSMUST00000027331; ENSMUSP00000027331; ENSMUSG00000026149.
DR GeneID; 66261; -.
DR KEGG; mmu:66261; -.
DR UCSC; uc007bsd.1; mouse.
DR CTD; 79853; -.
DR MGI; MGI:1913511; Tm4sf20.
DR VEuPathDB; HostDB:ENSMUSG00000026149; -.
DR eggNOG; ENOG502RZTZ; Eukaryota.
DR GeneTree; ENSGT01030000234590; -.
DR HOGENOM; CLU_105103_0_0_1; -.
DR InParanoid; Q9CQY8; -.
DR OMA; FDLQWFF; -.
DR OrthoDB; 1322314at2759; -.
DR PhylomeDB; Q9CQY8; -.
DR TreeFam; TF331371; -.
DR BioGRID-ORCS; 66261; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9CQY8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CQY8; protein.
DR Bgee; ENSMUSG00000026149; Expressed in duodenum and 60 other tissues.
DR Genevisible; Q9CQY8; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISS:UniProtKB.
DR InterPro; IPR008661; L6_membrane.
DR PANTHER; PTHR14198; PTHR14198; 1.
DR Pfam; PF05805; L6_membrane; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..226
FT /note="Transmembrane 4 L6 family member 20"
FT /id="PRO_0000251229"
FT TOPO_DOM 1..14
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..83
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..226
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT SITE 13..14
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q53R12"
FT CONFLICT 78
FT /note="C -> G (in Ref. 1; BAB30618)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="S -> I (in Ref. 1; BAB30635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 24760 MW; 3FE6BA1C6A335EAD CRC64;
MTCCEGWTSC NGFSLLILIL LGVVINCIPL GISLVEADST SQNPISCYEW WFPGIIGAGL
MAIPATTMSL AARKRACCNN KTGMFLSSLF SVITVVGAVY CMLVSLQALL EGPLICNTQA
NSTVTCEFSL KNLSKFDPES FNLLWFFNGT CVSPTDFKNP TINNMVSNWK IPNSNSEEDR
HRIFHFSVFM SLLLVGILEL LFGLSQILIG FLGCLCGVSQ RRSQIV
