TM119_HUMAN
ID TM119_HUMAN Reviewed; 283 AA.
AC Q4V9L6; Q6UXE5; Q8N2F5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Transmembrane protein 119;
DE AltName: Full=Osteoblast induction factor;
DE Short=OBIF;
DE Flags: Precursor;
GN Name=TMEM119; ORFNames=PSEC0199, UNQ731/PRO1415;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-72.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-72.
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Chondrosarcoma;
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).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20025746; DOI=10.1186/1471-213x-9-70;
RA Kanamoto T., Mizuhashi K., Terada K., Minami T., Yoshikawa H., Furukawa T.;
RT "Isolation and characterization of a novel plasma membrane protein,
RT osteoblast induction factor (obif), associated with osteoblast
RT differentiation.";
RL BMC Dev. Biol. 9:70-70(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26250788; DOI=10.1111/neup.12235;
RA Satoh J.I., Kino Y., Asahina N., Takitani M., Miyoshi J., Ishida T.,
RA Saito Y.;
RT "TMEM119 marks a subset of microglia in the human brain.";
RL Neuropathology 36:39-49(2016).
CC -!- FUNCTION: Plays an important role in bone formation and normal bone
CC mineralization. Promotes the differentiation of myoblasts into
CC osteoblasts (PubMed:20025746). May induce the commitment and
CC differentiation of myoblasts into osteoblasts through an enhancement of
CC BMP2 production and interaction with the BMP-RUNX2 pathway. Up-
CC regulates the expression of ATF4, a transcription factor which plays a
CC central role in osteoblast differentiation. Essential for normal
CC spermatogenesis and late testicular differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q8R138, ECO:0000269|PubMed:20025746}.
CC -!- SUBUNIT: Interacts with SMAD1, SMAD5 and RUNX2.
CC {ECO:0000250|UniProtKB:Q8R138}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20025746,
CC ECO:0000269|PubMed:26250788}; Single-pass type I membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8R138}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q8R138}.
CC -!- TISSUE SPECIFICITY: Expressed in brain microglia (at protein level).
CC Elevated expression levels seen in the brain of patients with Alzheimer
CC disease. Expressed by osteoblast-like cells in bone tissues and
CC follicular dendritic cells in lymphoid tissues.
CC {ECO:0000269|PubMed:26250788}.
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DR EMBL; AY358389; AAQ88755.1; -; mRNA.
DR EMBL; AK075501; BAC11656.1; -; mRNA.
DR EMBL; BC096825; AAH96825.1; -; mRNA.
DR CCDS; CCDS9119.1; -.
DR RefSeq; NP_859075.2; NM_181724.2.
DR RefSeq; XP_011536573.1; XM_011538271.2.
DR AlphaFoldDB; Q4V9L6; -.
DR BioGRID; 130795; 7.
DR IntAct; Q4V9L6; 1.
DR MINT; Q4V9L6; -.
DR STRING; 9606.ENSP00000376553; -.
DR TCDB; 9.B.413.1.1; the tmem119 (tmem119) family.
DR GlyGen; Q4V9L6; 1 site.
DR iPTMnet; Q4V9L6; -.
DR PhosphoSitePlus; Q4V9L6; -.
DR BioMuta; TMEM119; -.
DR DMDM; 74754588; -.
DR jPOST; Q4V9L6; -.
DR MassIVE; Q4V9L6; -.
DR MaxQB; Q4V9L6; -.
DR PaxDb; Q4V9L6; -.
DR PeptideAtlas; Q4V9L6; -.
DR PRIDE; Q4V9L6; -.
DR ProteomicsDB; 62285; -.
DR TopDownProteomics; Q4V9L6; -.
DR Antibodypedia; 55081; 30 antibodies from 12 providers.
DR DNASU; 338773; -.
DR Ensembl; ENST00000392806.4; ENSP00000376553.3; ENSG00000183160.9.
DR GeneID; 338773; -.
DR KEGG; hsa:338773; -.
DR MANE-Select; ENST00000392806.4; ENSP00000376553.3; NM_181724.3; NP_859075.2.
DR UCSC; uc001tng.4; human.
DR CTD; 338773; -.
DR DisGeNET; 338773; -.
DR GeneCards; TMEM119; -.
DR HGNC; HGNC:27884; TMEM119.
DR HPA; ENSG00000183160; Tissue enhanced (cervix).
DR MIM; 618989; gene.
DR neXtProt; NX_Q4V9L6; -.
DR OpenTargets; ENSG00000183160; -.
DR PharmGKB; PA143485640; -.
DR VEuPathDB; HostDB:ENSG00000183160; -.
DR eggNOG; ENOG502S283; Eukaryota.
DR GeneTree; ENSGT00390000017134; -.
DR HOGENOM; CLU_086693_0_0_1; -.
DR InParanoid; Q4V9L6; -.
DR OMA; EEPCSGV; -.
DR OrthoDB; 1284233at2759; -.
DR PhylomeDB; Q4V9L6; -.
DR TreeFam; TF336958; -.
DR PathwayCommons; Q4V9L6; -.
DR SignaLink; Q4V9L6; -.
DR BioGRID-ORCS; 338773; 18 hits in 1063 CRISPR screens.
DR ChiTaRS; TMEM119; human.
DR GenomeRNAi; 338773; -.
DR Pharos; Q4V9L6; Tbio.
DR PRO; PR:Q4V9L6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q4V9L6; protein.
DR Bgee; ENSG00000183160; Expressed in stromal cell of endometrium and 156 other tissues.
DR ExpressionAtlas; Q4V9L6; baseline and differential.
DR Genevisible; Q4V9L6; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0001958; P:endochondral ossification; ISS:ARUK-UCL.
DR GO; GO:0045779; P:negative regulation of bone resorption; ISS:ARUK-UCL.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:ARUK-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:1903012; P:positive regulation of bone development; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:ARUK-UCL.
DR GO; GO:0048515; P:spermatid differentiation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR031453; TMEM119.
DR PANTHER; PTHR28645; PTHR28645; 1.
DR Pfam; PF15724; TMEM119; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cell membrane; Cytoplasm; Differentiation;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Osteogenesis;
KW Phosphoprotein; Reference proteome; Signal; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..283
FT /note="Transmembrane protein 119"
FT /id="PRO_0000251220"
FT TOPO_DOM 26..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 43..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 41
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q8R138"
FT VARIANT 72
FT /note="I -> T (in dbSNP:rs7975237)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:16303743"
FT /id="VAR_027663"
FT CONFLICT 262
FT /note="E -> G (in Ref. 2; BAC11656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 29203 MW; 8676B7A11C06B569 CRC64;
MVSAAAPSLL ILLLLLLGSV PATDARSVPL KATFLEDVAG SGEAEGSSAS SPSLPPPWTP
ALSPTSMGPQ PITLGGPSPP TNFLDGIVDF FRQYVMLIAV VGSLAFLLMF IVCAAVITRQ
KQKASAYYPS SFPKKKYVDQ SDRAGGPRAF SEVPDRAPDS RPEEALDSSR QLQADILAAT
QNLKSPTRAA LGGGDGARMV EGRGAEEEEK GSQEGDQEVQ GHGVPVETPE AQEEPCSGVL
EGAVVAGEGQ GELEGSLLLA QEAQGPVGPP ESPCACSSVH PSV
