ID   TMM43_PONAB             Reviewed;         400 AA.
AC   Q5R9S8;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Transmembrane protein 43;
DE   AltName: Full=Protein LUMA;
GN   Name=TMEM43;
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=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May have an important role in maintaining nuclear envelope
CC       structure by organizing protein complexes at the inner nuclear
CC       membrane. Required for retaining emerin at the inner nuclear membrane
CC       (By similarity). Plays a role in the modulation of innate immune
CC       signaling through the cGAS-STING pathway by interacting with RNF26 (By
CC       similarity). In addition, functions as a critical signaling component
CC       in mediating NF-kappa-B activation by acting downstream of EGFR and
CC       upstream of CARD10 (By similarity). {ECO:0000250|UniProtKB:Q9BTV4}.
CC   -!- SUBUNIT: Can form oligomers through the transmembrane domains.
CC       Interacts with EMD; the interaction retains EMD at the inner nuclear
CC       membrane. Interacts with LMNA and LMNB2 (By similarity). Interacts with
CC       SUN2. Interacts with RNF26; this interaction is important to modulate
CC       innate immune signaling through the cGAS-STING pathway. Interacts with
CC       CARD10 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9BTV4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9BTV4}. Nucleus inner membrane
CC       {ECO:0000250|UniProtKB:Q9BTV4}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9BTV4}. Note=Retained in the inner nuclear
CC       membrane through interaction with EMD and A- and B-lamins. The N- and
CC       C-termini are oriented towards the nucleoplasm. The majority of the
CC       hydrophilic domain resides in the endoplasmic reticulum lumen (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TMEM43 family. {ECO:0000305}.
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DR   EMBL; CR859304; CAH91482.1; -; mRNA.
DR   EMBL; CR926103; CAI29729.1; -; mRNA.
DR   RefSeq; NP_001125873.1; NM_001132401.1.
DR   AlphaFoldDB; Q5R9S8; -.
DR   STRING; 9601.ENSPPYP00000014987; -.
DR   Ensembl; ENSPPYT00000015587; ENSPPYP00000014987; ENSPPYG00000013400.
DR   GeneID; 100172804; -.
DR   KEGG; pon:100172804; -.
DR   CTD; 79188; -.
DR   eggNOG; ENOG502QSR2; Eukaryota.
DR   GeneTree; ENSGT00390000009671; -.
DR   HOGENOM; CLU_042602_1_0_1; -.
DR   InParanoid; Q5R9S8; -.
DR   OMA; DWFPVVR; -.
DR   OrthoDB; 866982at2759; -.
DR   TreeFam; TF324718; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0071763; P:nuclear membrane organization; IEA:Ensembl.
DR   InterPro; IPR012430; TMEM43_fam.
DR   PANTHER; PTHR13416; PTHR13416; 1.
DR   Pfam; PF07787; TMEM43; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; Immunity; Innate immunity; Membrane;
KW   Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTV4"
FT   CHAIN           2..400
FT                   /note="Transmembrane protein 43"
FT                   /id="PRO_0000284500"
FT   TOPO_DOM        2..31
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..313
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..345
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..368
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..400
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTV4"
SQ   SEQUENCE   400 AA;  44987 MW;  BF18B74AEE911DF7 CRC64;
     MAANYSSTST RREHVKVKTG SQPGFLERLS ETWGGMFVGL MAFLLSFYLI FTNEGRALKT
     ATSLAEGLSL VVSPDSIHSV APENEGRLVH IIGALRTSKL LSDPNYGVHL PAVKLRRHVE
     MYQWVETEES REYTEDEQVK KETRYSYNTE WRSEIINSKN FDREIGHKNP SAMAVESFTA
     TAPFVQIGRF FLSSGLIDKV DNFKSLSLSK LEDPHVDIIR RGDFFYHSEN PKYPEVGDLR
     VSFSYAGLSG DDPDLGPAHV VTVIARQRGD QLVPFSTKSG DTLLLLHHGD FSAEEVFHRE
     LRSNSMKTWG LRAAGWMAMF MGLNLMTRIL YTLVDWFPVF RDLVNIGLKA FAFCVATSLT
     LLTVAAGWLF YRPLWALLIA GLALVPIIVA RTRVPAKKLE