ID   TM199_RAT               Reviewed;         208 AA.
AC   Q5BK13;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Transmembrane protein 199;
GN   Name=Tmem199;
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=Spleen;
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: Accessory component of the proton-transporting vacuolar (V)-
CC       ATPase protein pump involved in intracellular iron homeostasis. In
CC       aerobic conditions, required for intracellular iron homeostasis, thus
CC       triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and
CC       leading to HIF1A hydroxylation and subsequent proteasomal degradation.
CC       Necessary for endolysosomal acidification and lysosomal degradation (By
CC       similarity). May be involved in Golgi homeostasis (By similarity).
CC       {ECO:0000250|UniProtKB:Q8N511}.
CC   -!- SUBUNIT: Accessory component of the multisubunit proton-transporting
CC       vacuolar (V)-ATPase protein pump. {ECO:0000250|UniProtKB:Q8N511}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250|UniProtKB:Q8N511}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC       membrane {ECO:0000250|UniProtKB:Q8N511}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8N511}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Partial colocalization with GOLGB1.
CC       {ECO:0000250|UniProtKB:Q8N511}.
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DR   EMBL; BC091246; AAH91246.1; -; mRNA.
DR   RefSeq; NP_001020163.1; NM_001024992.1.
DR   AlphaFoldDB; Q5BK13; -.
DR   STRING; 10116.ENSRNOP00000013220; -.
DR   PaxDb; Q5BK13; -.
DR   GeneID; 303332; -.
DR   KEGG; rno:303332; -.
DR   CTD; 147007; -.
DR   RGD; 1566425; Tmem199.
DR   VEuPathDB; HostDB:ENSRNOG00000009896; -.
DR   eggNOG; ENOG502RXKD; Eukaryota.
DR   HOGENOM; CLU_114590_0_0_1; -.
DR   InParanoid; Q5BK13; -.
DR   OMA; DFGQQVR; -.
DR   OrthoDB; 1216090at2759; -.
DR   PhylomeDB; Q5BK13; -.
DR   TreeFam; TF314610; -.
DR   PRO; PR:Q5BK13; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000009896; Expressed in quadriceps femoris and 20 other tissues.
DR   Genevisible; Q5BK13; RN.
DR   GO; GO:0030663; C:COPI-coated vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IEA:GOC.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISS:UniProtKB.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR   GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR   GO; GO:1905146; P:lysosomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:InterPro.
DR   InterPro; IPR021013; ATPase_Vma12.
DR   PANTHER; PTHR31394; PTHR31394; 1.
DR   Pfam; PF11712; Vma12; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N511"
FT   CHAIN           2..208
FT                   /note="Transmembrane protein 199"
FT                   /id="PRO_0000079301"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N511"
SQ   SEQUENCE   208 AA;  23160 MW;  473763582AF87B6A CRC64;
     MASSLLAGER LVRALDPGGE LEREQLPRKL RAQLEAALGK KHAGSDNATG PRRLVSFRLI
     RDLHQHLRER NSMLYLHELL EGSEIYFPEI VKPPRNPELV ARLEKIKIQL ANEEYKRITR
     NVTCQDAQCG GTLSDLGKQV RSVKALVITI FNFIVTVAAA FVCTYLGSQY IFTEMASRVL
     AALIVASVVG LAELYVMVRA MEGELGEL