ID   TEX2_HUMAN              Reviewed;        1127 AA.
AC   Q8IWB9; Q6AHZ5; Q8N3L0; Q9C0C5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Testis-expressed protein 2;
DE   AltName: Full=Transmembrane protein 96;
GN   Name=TEX2; Synonyms=KIAA1738, TMEM96;
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] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA   Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:347-355(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skeletal muscle, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-266; SER-270 AND
RP   SER-295, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-266 AND SER-732, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-295; SER-732;
RP   SER-738 AND SER-744, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22250200; DOI=10.1242/jcs.085118;
RA   Toulmay A., Prinz W.A.;
RT   "A conserved membrane-binding domain targets proteins to organelle contact
RT   sites.";
RL   J. Cell Sci. 125:49-58(2012).
RN   [10]
RP   FUNCTION.
RX   PubMed=28011845; DOI=10.1083/jcb.201606059;
RA   Liu L.K., Choudhary V., Toulmay A., Prinz W.A.;
RT   "An inducible ER-Golgi tether facilitates ceramide transport to alleviate
RT   lipotoxicity.";
RL   J. Cell Biol. 216:131-147(2017).
CC   -!- FUNCTION: During endoplasmic reticulum (ER) stress or when cellular
CC       ceramide levels increase, may induce contacts between the ER and
CC       medial-Golgi complex to facilitate non-vesicular transport of ceramides
CC       from the ER to the Golgi complex where they are converted to complex
CC       sphingolipids, preventing toxic ceramide accumulation.
CC       {ECO:0000269|PubMed:28011845}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein
CC       {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi-
CC       pass membrane protein {ECO:0000255}. Note=Enriched at the nucleus-
CC       vacuole junction (PubMed:22250200). During endoplasmic reticulum (ER)
CC       stress, localizes to ER-Golgi contacts (By similarity).
CC       {ECO:0000250|UniProtKB:Q06833, ECO:0000269|PubMed:22250200}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IWB9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IWB9-2; Sequence=VSP_019569;
CC   -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC       various types of glycerophospholipids in its interior and mediate their
CC       transfer between two adjacent bilayers. {ECO:0000255|PROSITE-
CC       ProRule:PRU01194}.
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DR   EMBL; AB051525; BAB21829.2; -; mRNA.
DR   EMBL; AL834251; CAD38927.1; -; mRNA.
DR   EMBL; CR627433; CAH10519.1; -; mRNA.
DR   EMBL; BC040521; AAH40521.1; -; mRNA.
DR   CCDS; CCDS11658.1; -. [Q8IWB9-2]
DR   CCDS; CCDS74131.1; -. [Q8IWB9-1]
DR   RefSeq; NP_001275661.1; NM_001288732.1. [Q8IWB9-1]
DR   RefSeq; NP_001275662.1; NM_001288733.1. [Q8IWB9-1]
DR   RefSeq; NP_060939.3; NM_018469.4. [Q8IWB9-2]
DR   RefSeq; XP_011523300.1; XM_011524998.1. [Q8IWB9-2]
DR   RefSeq; XP_011523301.1; XM_011524999.1. [Q8IWB9-2]
DR   AlphaFoldDB; Q8IWB9; -.
DR   BioGRID; 120954; 188.
DR   DIP; DIP-47321N; -.
DR   IntAct; Q8IWB9; 15.
DR   MINT; Q8IWB9; -.
DR   STRING; 9606.ENSP00000258991; -.
DR   GlyCosmos; Q8IWB9; 3 sites, 1 glycan.
DR   GlyGen; Q8IWB9; 5 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q8IWB9; -.
DR   PhosphoSitePlus; Q8IWB9; -.
DR   BioMuta; TEX2; -.
DR   DMDM; 109895136; -.
DR   EPD; Q8IWB9; -.
DR   jPOST; Q8IWB9; -.
DR   MassIVE; Q8IWB9; -.
DR   MaxQB; Q8IWB9; -.
DR   PaxDb; 9606-ENSP00000258991; -.
DR   PeptideAtlas; Q8IWB9; -.
DR   ProteomicsDB; 70839; -. [Q8IWB9-1]
DR   ProteomicsDB; 70840; -. [Q8IWB9-2]
DR   Pumba; Q8IWB9; -.
DR   Antibodypedia; 19114; 106 antibodies from 23 providers.
DR   DNASU; 55852; -.
DR   Ensembl; ENST00000258991.7; ENSP00000258991.3; ENSG00000136478.9. [Q8IWB9-2]
DR   Ensembl; ENST00000583097.5; ENSP00000462665.1; ENSG00000136478.9. [Q8IWB9-1]
DR   Ensembl; ENST00000584379.6; ENSP00000463001.1; ENSG00000136478.9. [Q8IWB9-1]
DR   GeneID; 55852; -.
DR   KEGG; hsa:55852; -.
DR   MANE-Select; ENST00000584379.6; ENSP00000463001.1; NM_001288732.2; NP_001275661.1.
DR   UCSC; uc002jec.5; human. [Q8IWB9-1]
DR   AGR; HGNC:30884; -.
DR   CTD; 55852; -.
DR   DisGeNET; 55852; -.
DR   GeneCards; TEX2; -.
DR   HGNC; HGNC:30884; TEX2.
DR   HPA; ENSG00000136478; Low tissue specificity.
DR   MIM; 619929; gene.
DR   neXtProt; NX_Q8IWB9; -.
DR   OpenTargets; ENSG00000136478; -.
DR   PharmGKB; PA142670820; -.
DR   VEuPathDB; HostDB:ENSG00000136478; -.
DR   eggNOG; KOG2238; Eukaryota.
DR   GeneTree; ENSGT00390000000463; -.
DR   HOGENOM; CLU_008315_0_0_1; -.
DR   InParanoid; Q8IWB9; -.
DR   OMA; KRWNTGA; -.
DR   OrthoDB; 25570at2759; -.
DR   PhylomeDB; Q8IWB9; -.
DR   TreeFam; TF314900; -.
DR   PathwayCommons; Q8IWB9; -.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   SignaLink; Q8IWB9; -.
DR   BioGRID-ORCS; 55852; 36 hits in 1155 CRISPR screens.
DR   ChiTaRS; TEX2; human.
DR   GenomeRNAi; 55852; -.
DR   Pharos; Q8IWB9; Tbio.
DR   PRO; PR:Q8IWB9; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q8IWB9; Protein.
DR   Bgee; ENSG00000136478; Expressed in medial globus pallidus and 204 other cell types or tissues.
DR   ExpressionAtlas; Q8IWB9; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   GO; GO:0006665; P:sphingolipid metabolic process; NAS:UniProtKB.
DR   CDD; cd21675; SMP_TEX2; 1.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR13466:SF2; TESTIS-EXPRESSED PROTEIN 2; 1.
DR   PANTHER; PTHR13466; TEX2 PROTEIN-RELATED; 1.
DR   PROSITE; PS51847; SMP; 1.
DR   Genevisible; Q8IWB9; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Lipid transport;
KW   Lipid-binding; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1127
FT                   /note="Testis-expressed protein 2"
FT                   /id="PRO_0000244479"
FT   TRANSMEM        475..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        497..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          816..1101
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..804
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         262
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT   MOD_RES         732
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         738
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         744
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         748
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT   MOD_RES         751
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT   MOD_RES         815
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         724
FT                   /note="K -> KPAPVFLA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019569"
FT   VARIANT         158
FT                   /note="T -> I (in dbSNP:rs28605685)"
FT                   /id="VAR_061712"
FT   CONFLICT        53
FT                   /note="R -> K (in Ref. 3; AAH40521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="N -> S (in Ref. 2; CAD38927)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="P -> S (in Ref. 2; CAH10519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        451
FT                   /note="E -> K (in Ref. 3; AAH40521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        608
FT                   /note="I -> V (in Ref. 2; CAD38927)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        634
FT                   /note="P -> L (in Ref. 2; CAD38927)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        725..729
FT                   /note="PGLLP -> LRAFA (in Ref. 2; CAH10519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        835
FT                   /note="F -> S (in Ref. 2; CAD38927)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1127 AA;  125303 MW;  100D99905117CD57 CRC64;
     MTSLYGRHAE KTTDMPKPSA PKVHVQRSVS RDTIAIHFSA SGEEEEEEEE EFREYFEEGL
     DDQSIVTGLE AKEDLYLEPQ VGHDPAGPAA SPVLADGLSV SQAPAILPVS KNTVKLLESP
     VPAAQVLSTV PLAVSPGSSS SGPLASSPSV SSLSEQKTSS SSPLSSPSKS PILSSSASTS
     TLSSAKPFMS LVKSLSTEVE PKESPHPARH RHLMKTLVKS LSTDTSRQES DTVSYKPPDS
     KLNLHLFKQF TQPRNTGGDS KTAPSSPLTS PSDTRSFFKV PEMEAKIEDT KRRLSEVIYE
     PFQLLSKIIG EESGSHRPKA LSSSASELSN LSSLNGHLES NNNYSIKEEE CDSEGDGYGS
     DSNIPRSDHP KSTGEPTREI ELKSSQGSSL KDLGLKTSSL VLEKCSLSAL VSKEDEEFCE
     LYTEDFDLET EGESKVDKLS DIPLKPEVLA EDGVVLDSED EVDSAVQHPE LPVKTLGFFI
     MCVYVYLILP LPHYVSGLFL GIGLGFMTAV CVIWFFTPPS AHKYHKLHKN LRHWNTRSLD
     IKEPEILKGW MNEIYNYDPE TYHATLTHSV FVRLEGGTLR LSKPNKNISR RASYNEPKPE
     VTYISQKIYD LSDSKIYLVP KTLARKRIWN KKYPICIELG QQDDFMSKAQ TDKETSEEKP
     PAEGSEDPKK PPRPQEGTRS SQRDQILYLF GRTGREKEEW FRRFILASKL KSEIKKSSGV
     SGGKPGLLPA HSRHNSPSGH LTHSRSSSKG SVEEIMSQPK QKELAGSVRQ KMLLDYSVYM
     GRCVPQESRS PQRSPLQSAE SSPTAGKKLP EVPPSEEEEQ EAWVNALLGR IFWDFLGEKY
     WSDLVSKKIQ MKLSKIKLPY FMNELTLTEL DMGVAVPKIL QAFKPYVDHQ GLWIDLEMSY
     NGSFLMTLET KMNLTKLGKE PLVEALKVGE IGKEGCRPRA FCLADSDEES SSAGSSEEDD
     APEPSGGDKQ LLPGAEGYVG GHRTSKIMRF VDKITKSKYF QKATETEFIK KKIEEVSNTP
     LLLTVEVQEC RGTLAVNIPP PPTDRVWYGF RKPPHVELKA RPKLGEREVT LVHVTDWIEK
     KLEQEFQKVF VMPNMDDVYI TIMHSAMDPR STSCLLKDPP VEAADQP
//