ID   T4S20_BOVIN             Reviewed;         230 AA.
AC   Q3T0Z4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Transmembrane 4 L6 family member 20;
GN   Name=TM4SF20;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 in presence of ceramide which inverts the
CC       orientation of TM4SF20 in membranes exposing these residues to the
CC       endoplasmic reticulum lumen. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC102196; AAI02197.1; -; mRNA.
DR   RefSeq; NP_001070449.1; NM_001076981.1.
DR   AlphaFoldDB; Q3T0Z4; -.
DR   STRING; 9913.ENSBTAP00000028426; -.
DR   PaxDb; Q3T0Z4; -.
DR   GeneID; 767902; -.
DR   KEGG; bta:767902; -.
DR   CTD; 79853; -.
DR   eggNOG; ENOG502RZTZ; Eukaryota.
DR   InParanoid; Q3T0Z4; -.
DR   OrthoDB; 1322314at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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..230
FT                   /note="Transmembrane 4 L6 family member 20"
FT                   /id="PRO_0000251227"
FT   TOPO_DOM        1..11
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..44
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..83
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..230
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   SITE            13..14
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q53R12"
SQ   SEQUENCE   230 AA;  25214 MW;  FF48895B0B2F6932 CRC64;
     MTCCEGWTSC NGFSLLVLLL LGVTLNAIPL ILNFVDEDQF FENPISCFEW WFPGIIGAGV
     MAIPATTMSL AARKRACCNN KTGMFLSSLL NAITVIGAAY CLLVSIQALA EGPLICNSQS
     NTTSSCEFSL KNLTANYKES FDLQWFFEDS CVPHTDSNNP SITNTTANNW RVYNLHFNSI
     ENQHRIIHFS VFLGLLLVGI LEILFGLSQI IIGFFGCLCG GVSNGRSQIV