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Transmembrane and immunoglobulin domain-containing protein 2 (CD28 homolog) (Immunoglobulin and proline-rich receptor 1) (IGPR-1)

 TMIG2_HUMAN             Reviewed;         282 AA.
Q96BF3; Q6UW59;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
12-SEP-2018, entry version 133.
RecName: Full=Transmembrane and immunoglobulin domain-containing protein 2;
AltName: Full=CD28 homolog;
AltName: Full=Immunoglobulin and proline-rich receptor 1;
Short=IGPR-1;
Flags: Precursor;
Name=TMIGD2; Synonyms=CD28H, IGPR1; ORFNames=UNQ3059/PRO9879;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-202.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 23-37.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[5]
FUNCTION, INTERACTION WITH CACNB2; DST; MIA AND NCKIPSD, SUBCELLULAR
LOCATION, HOMOPHILIC INTERACTION, TISSUE SPECIFICITY, AND
GLYCOSYLATION.
PubMed=22419821; DOI=10.1091/mbc.E11-11-0934;
Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.;
"Identification of IGPR-1 as a novel adhesion molecule involved in
angiogenesis.";
Mol. Biol. Cell 23:1646-1656(2012).
[6]
FUNCTION IN T-CELL COSTIMULATION, INTERACTION WITH HHLA2, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, PROBABLE PHOSPHORYLATION AT TYR-192
AND TYR-222, AND MUTAGENESIS OF TYR-192; TYR-197 AND TYR-222.
PubMed=23784006; DOI=10.1038/ncomms3043;
Zhu Y., Yao S., Iliopoulou B.P., Han X., Augustine M.M., Xu H.,
Phennicie R.T., Flies S.J., Broadwater M., Ruff W., Taube J.M.,
Zheng L., Luo L., Zhu G., Chen J., Chen L.;
"B7-H5 costimulates human T cells via CD28H.";
Nat. Commun. 4:2043-2043(2013).
-!- FUNCTION: Plays a role in cell-cell interaction, cell migration,
and angiogenesis. Through interaction with HHLA2, costimulates T-
cells in the context of TCR-mediated activation. Enhances T-cell
proliferation and cytokine production via an AKT-dependent
signaling cascade. {ECO:0000269|PubMed:22419821,
ECO:0000269|PubMed:23784006}.
-!- SUBUNIT: May form homophilic interactions that could regulate
cell-cell interaction. Interacts with CACNB2, DST, MIA and
NCKIPSD. Interacts with HHLA2. {ECO:0000269|PubMed:22419821,
ECO:0000269|PubMed:23784006}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22419821};
Single-pass type I membrane protein {ECO:0000269|PubMed:22419821}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96BF3-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q96BF3-2; Sequence=VSP_022967;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, mainly by epithelial and
endothelial cells, including bronchial epithelial cells of lung,
breast glandular and lobular epithelia cells, urothelium of the
bladder, skin epidermis, epithelium of gastrointestinal, rectum,
endometrial glands of the uterus, ureter, fallopian tube
epithelium, colonic epithelium, small bowl epithelium, stomach
epithelium, including both chief and parietal cells, trophoblastic
epithelium of placenta, and pancreatic acinar cells (at protein
level). Consistently expressed in veins and arteries (at protein
level). Not detected in thyroid, cerebellum, cerebral cortex and
thymus (at protein level). Expressed in lymphoid organs, with
highest levels in thymus, spleen, peripheral blood lymphocytes and
liver. In the thymus, expressed in CD4+ and CD8+ single- and
double-positive cells, but not in immature CD4- and CD8- double-
negative cells (at protein level). In peripheral blood mononuclear
cells, highly expressed on CD56+ or CD16+ natural killer cells and
CD3+ T-cells(at protein level). Not detected on B-cells(at protein
level). Expressed in tonsils (at protein level).
{ECO:0000269|PubMed:22419821, ECO:0000269|PubMed:23784006}.
-!- DEVELOPMENTAL STAGE: Repetitive stimulation of naive T-cells,
including with IL2 and antibodies against CD3 and CD28 or
repetitive antigenic exposure, leads to progressive and
irreversible loss of expression. {ECO:0000269|PubMed:23784006}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:22419821}.
-----------------------------------------------------------------------
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EMBL; AY358964; AAQ89323.1; -; mRNA.
EMBL; BC015655; AAH15655.1; -; mRNA.
CCDS; CCDS12126.1; -. [Q96BF3-1]
CCDS; CCDS59334.1; -. [Q96BF3-2]
RefSeq; NP_001162597.1; NM_001169126.1. [Q96BF3-2]
RefSeq; NP_001295161.1; NM_001308232.1.
RefSeq; NP_653216.2; NM_144615.2. [Q96BF3-1]
UniGene; Hs.263928; -.
ProteinModelPortal; Q96BF3; -.
BioGrid; 125971; 1.
iPTMnet; Q96BF3; -.
PhosphoSitePlus; Q96BF3; -.
SwissPalm; Q96BF3; -.
BioMuta; TMIGD2; -.
DMDM; 125991218; -.
PaxDb; Q96BF3; -.
PeptideAtlas; Q96BF3; -.
PRIDE; Q96BF3; -.
ProteomicsDB; 76072; -.
ProteomicsDB; 76073; -. [Q96BF3-2]
Ensembl; ENST00000301272; ENSP00000301272; ENSG00000167664. [Q96BF3-1]
Ensembl; ENST00000595645; ENSP00000470561; ENSG00000167664. [Q96BF3-2]
GeneID; 126259; -.
KEGG; hsa:126259; -.
UCSC; uc002lzx.3; human. [Q96BF3-1]
CTD; 126259; -.
DisGeNET; 126259; -.
EuPathDB; HostDB:ENSG00000167664.8; -.
GeneCards; TMIGD2; -.
H-InvDB; HIX0014660; -.
HGNC; HGNC:28324; TMIGD2.
HPA; HPA011081; -.
MIM; 614715; gene.
neXtProt; NX_Q96BF3; -.
OpenTargets; ENSG00000167664; -.
PharmGKB; PA145148047; -.
eggNOG; ENOG410J9M6; Eukaryota.
eggNOG; ENOG41118HW; LUCA.
GeneTree; ENSGT00390000007100; -.
HOGENOM; HOG000154641; -.
InParanoid; Q96BF3; -.
KO; K16668; -.
OMA; YSNVLYR; -.
OrthoDB; EOG091G0MZN; -.
PhylomeDB; Q96BF3; -.
TreeFam; TF341425; -.
GenomeRNAi; 126259; -.
PRO; PR:Q96BF3; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167664; Expressed in 190 organ(s), highest expression level in quadriceps femoris.
CleanEx; HS_TMIGD2; -.
ExpressionAtlas; Q96BF3; baseline and differential.
Genevisible; Q96BF3; HS.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0015026; F:coreceptor activity; IDA:UniProtKB.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0002377; P:immunoglobulin production; IBA:GO_Central.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:CACAO.
GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000269|PubMed:15340161}.
CHAIN 23 282 Transmembrane and immunoglobulin domain-
containing protein 2.
/FTId=PRO_0000275870.
TOPO_DOM 23 150 Extracellular. {ECO:0000255}.
TRANSMEM 151 171 Helical. {ECO:0000255}.
TOPO_DOM 172 282 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 129 Ig-like.
COMPBIAS 227 277 Pro-rich.
MOD_RES 192 192 Phosphotyrosine. {ECO:0000305}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 222 222 Phosphotyrosine. {ECO:0000305}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 112 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 186 189 Missing (in isoform 2).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_022967.
VARIANT 168 168 W -> L (in dbSNP:rs58237134).
/FTId=VAR_061328.
VARIANT 202 202 A -> P (in dbSNP:rs28477168).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030469.
MUTAGEN 192 192 Y->F: Partial loss of phosphorylation;
when associated with F-197. Complete loss
of phosphorylation; when associated with
F-222. {ECO:0000269|PubMed:23784006}.
MUTAGEN 197 197 Y->F: Partial loss of phosphorylation;
when associated with F-192 or with F-222.
{ECO:0000269|PubMed:23784006}.
MUTAGEN 222 222 Y->F: Partial loss of phosphorylation;
when tested individually or when
associated with F-197. Complete loss of
phosphorylation; when associated with F-
192. {ECO:0000269|PubMed:23784006}.
SEQUENCE 282 AA; 30675 MW; AABB3FFD840B44DC CRC64;
MGSPGMVLGL LVQIWALQEA SSLSVQQGPN LLQVRQGSQA TLVCQVDQAT AWERLRVKWT
KDGAILCQPY ITNGSLSLGV CGPQGRLSWQ APSHLTLQLD PVSLNHSGAY VCWAAVEIPE
LEEAEGNITR LFVDPDDPTQ NRNRIASFPG FLFVLLGVGS MGVAAIVWGA WFWGRRSCQQ
RDSGNSPGNA FYSNVLYRPR GAPKKSEDCS GEGKDQRGQS IYSTSFPQPA PRQPHLASRP
CPSPRPCPSP RPGHPVSMVR VSPRPSPTQQ PRPKGFPKVG EE


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