ID   TMM43_RAT               Reviewed;         400 AA.
AC   Q5XIP9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Transmembrane protein 43;
DE   AltName: Full=Protein LUMA;
GN   Name=Tmem43;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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: 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). Contributes to passive conductance
CC       current in cochlear glia-like supporting cells, mediated by gap
CC       junctions and necessary for hearing (By similarity).
CC       {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). Interacts with gap junctions proteins GJB2/Cx26
CC       and GJB4/Cx30 (By similarity). {ECO:0000250,
CC       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}. Cell membrane
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; BC083626; AAH83626.1; -; mRNA.
DR   RefSeq; NP_001007746.1; NM_001007745.1.
DR   AlphaFoldDB; Q5XIP9; -.
DR   BioGRID; 263420; 1.
DR   IntAct; Q5XIP9; 2.
DR   STRING; 10116.ENSRNOP00000010895; -.
DR   PhosphoSitePlus; Q5XIP9; -.
DR   jPOST; Q5XIP9; -.
DR   PaxDb; 10116-ENSRNOP00000010895; -.
DR   Ensembl; ENSRNOT00055006914; ENSRNOP00055005196; ENSRNOG00055004349.
DR   Ensembl; ENSRNOT00060047611; ENSRNOP00060039608; ENSRNOG00060027304.
DR   Ensembl; ENSRNOT00065042438; ENSRNOP00065034724; ENSRNOG00065024642.
DR   GeneID; 362401; -.
DR   KEGG; rno:362401; -.
DR   AGR; RGD:1549711; -.
DR   CTD; 79188; -.
DR   RGD; 1549711; Tmem43.
DR   VEuPathDB; HostDB:ENSRNOG00000007519; -.
DR   eggNOG; ENOG502QSR2; Eukaryota.
DR   HOGENOM; CLU_042602_1_0_1; -.
DR   InParanoid; Q5XIP9; -.
DR   OrthoDB; 3663310at2759; -.
DR   PhylomeDB; Q5XIP9; -.
DR   TreeFam; TF324718; -.
DR   PRO; PR:Q5XIP9; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000007519; Expressed in esophagus and 19 other cell types or tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0043621; F:protein self-association; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0071763; P:nuclear membrane organization; ISO:RGD.
DR   InterPro; IPR012430; TMEM43_fam.
DR   PANTHER; PTHR13416:SF2; TRANSMEMBRANE PROTEIN 43; 1.
DR   PANTHER; PTHR13416; UNCHARACTERIZED; 1.
DR   Pfam; PF07787; TMEM43; 1.
DR   Genevisible; Q5XIP9; RN.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Endoplasmic reticulum; Immunity;
KW   Innate immunity; Membrane; Nucleus; Reference proteome; Transmembrane;
KW   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_0000284501"
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   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTV4"
SQ   SEQUENCE   400 AA;  44774 MW;  5B1C68706DFD4E59 CRC64;
     MAANYSSTGS RKEHVKVTSD PQPGFLERLS ETSGGMFVGL VTFLLSFYLI FTNEGRALKT
     ANLLAEGLSL VVSPDSIHSV APENEGRLVH IIGALRTSKL LSDPNYGVHL PAVKLRRHVE
     MYQWVETEES NEYTEDGQVK KETKYSYNTE WRSEIVSSKN FDREIGHKNP SAMAVESFTA
     TAPFVQIGRF FLSAGLIDKI DNFKPLSLAK LEDPHVDIIR RGDFFYHSEN PKYPEVGDVR
     VSFSYAGLSS DDPDLGPAHV VTVIARQRGD QLIPYSTKSG DTLLLLHHGD FSAEEVFRRE
     QKSNSMKTWG LRAAGWMAMF MGLNLMTRIL YTLVDWFPVF RDLVNIGLKA FAFCVATSLT
     LLTVAAGWLF YRPLWAALLG CLALVPIIIA RTRVPTKKLE
//