ID   TM199_PONAB             Reviewed;         208 AA.
AC   Q5RAS8;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Transmembrane protein 199;
GN   Name=TMEM199;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In aerobic conditions, required for intracellular iron
CC       homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase
CC       (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent
CC       proteasomal degradation. Necessary for endolysosomal acidification and
CC       lysosomal degradation (By similarity). May be involved in Golgi
CC       homeostasis (By similarity). {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; CR858934; CAH91132.1; -; mRNA.
DR   RefSeq; NP_001125662.1; NM_001132190.1.
DR   AlphaFoldDB; Q5RAS8; -.
DR   STRING; 9601.ENSPPYP00000009097; -.
DR   Ensembl; ENSPPYT00000009467; ENSPPYP00000009097; ENSPPYG00000008090.
DR   GeneID; 100172582; -.
DR   KEGG; pon:100172582; -.
DR   CTD; 147007; -.
DR   eggNOG; ENOG502RXKD; Eukaryota.
DR   GeneTree; ENSGT00390000014591; -.
DR   HOGENOM; CLU_114590_0_0_1; -.
DR   InParanoid; Q5RAS8; -.
DR   OMA; DFGQQVR; -.
DR   OrthoDB; 1216090at2759; -.
DR   TreeFam; TF314610; -.
DR   Proteomes; UP000001595; Chromosome 17.
DR   GO; GO:0030663; C:COPI-coated vesicle membrane; ISS:UniProtKB.
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_0000079300"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
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;  23060 MW;  0DF06ABB2F7B7C42 CRC64;
     MASSLLAGER LVRALGPGGE LEPELLPRKL RAELEAALGK KHTGGDSSSG PQRLVSFRLI
     RDLHQHLRER DSKLYLHELL EGSEIYLPEV VKPPRNPELV ARLEKIKIQL ANEEYKRITR
     NVTCQDTRHG GTLSDLGKQV RSLKALVITI FNFIVTVVAA FVCTYLGSQY IFTEMASRVL
     AALIVASVVG LAELYVMVRA MEGELGEL