TMM43_RAT
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 03-AUG-2022, entry version 99.
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). {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; 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 jPOST; Q5XIP9; -.
DR PaxDb; Q5XIP9; -.
DR PRIDE; Q5XIP9; -.
DR GeneID; 362401; -.
DR KEGG; rno:362401; -.
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 OMA; DWFPVVR; -.
DR OrthoDB; 866982at2759; -.
DR PhylomeDB; Q5XIP9; -.
DR TreeFam; TF324718; -.
DR PRO; PR:Q5XIP9; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007519; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q5XIP9; RN.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; ISO:RGD.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
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:0071763; P:nuclear membrane organization; ISO:RGD.
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_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
