ID   TM131_HUMAN             Reviewed;        1883 AA.
AC   Q92545;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 3.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Transmembrane protein 131;
DE   AltName: Full=Protein RW1;
GN   Name=TMEM131; Synonyms=KIAA0257, RW1;
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 GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-1883.
RC   TISSUE=Bone marrow;
RX   PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA   Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA   Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. VI. The
RT   coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT   cDNA clones from cell line KG-1 and brain.";
RL   DNA Res. 3:321-329(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1863, AND IDENTIFICATION BY
RP   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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1375, 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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND SER-1863, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1322; SER-1375 AND SER-1871,
RP   AND IDENTIFICATION BY 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).
CC   -!- FUNCTION: May play a role in the immune response to viral infection.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TMEM131 family. {ECO:0000305}.
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DR   EMBL; AC079337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D87446; BAA13387.1; -; mRNA.
DR   CCDS; CCDS46368.1; -.
DR   RefSeq; NP_056163.1; NM_015348.1.
DR   AlphaFoldDB; Q92545; -.
DR   SMR; Q92545; -.
DR   BioGRID; 117052; 190.
DR   IntAct; Q92545; 27.
DR   MINT; Q92545; -.
DR   STRING; 9606.ENSP00000186436; -.
DR   GlyConnect; 1850; 4 N-Linked glycans (3 sites).
DR   GlyCosmos; Q92545; 4 sites, 3 glycans.
DR   GlyGen; Q92545; 9 sites, 3 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q92545; -.
DR   PhosphoSitePlus; Q92545; -.
DR   BioMuta; TMEM131; -.
DR   DMDM; 327478552; -.
DR   EPD; Q92545; -.
DR   jPOST; Q92545; -.
DR   MassIVE; Q92545; -.
DR   MaxQB; Q92545; -.
DR   PaxDb; 9606-ENSP00000186436; -.
DR   PeptideAtlas; Q92545; -.
DR   ProteomicsDB; 75306; -.
DR   Pumba; Q92545; -.
DR   Antibodypedia; 9002; 26 antibodies from 10 providers.
DR   DNASU; 23505; -.
DR   Ensembl; ENST00000186436.10; ENSP00000186436.5; ENSG00000075568.17.
DR   Ensembl; ENST00000708031.1; ENSP00000517074.1; ENSG00000291574.1.
DR   GeneID; 23505; -.
DR   KEGG; hsa:23505; -.
DR   MANE-Select; ENST00000186436.10; ENSP00000186436.5; NM_015348.2; NP_056163.1.
DR   UCSC; uc002syh.5; human.
DR   AGR; HGNC:30366; -.
DR   CTD; 23505; -.
DR   DisGeNET; 23505; -.
DR   GeneCards; TMEM131; -.
DR   HGNC; HGNC:30366; TMEM131.
DR   HPA; ENSG00000075568; Low tissue specificity.
DR   MIM; 615659; gene.
DR   neXtProt; NX_Q92545; -.
DR   OpenTargets; ENSG00000075568; -.
DR   PharmGKB; PA143485651; -.
DR   VEuPathDB; HostDB:ENSG00000075568; -.
DR   eggNOG; KOG3620; Eukaryota.
DR   GeneTree; ENSGT00530000063614; -.
DR   HOGENOM; CLU_002491_1_1_1; -.
DR   InParanoid; Q92545; -.
DR   OMA; NNFAMPL; -.
DR   OrthoDB; 2908591at2759; -.
DR   PhylomeDB; Q92545; -.
DR   TreeFam; TF321435; -.
DR   PathwayCommons; Q92545; -.
DR   SignaLink; Q92545; -.
DR   BioGRID-ORCS; 23505; 23 hits in 1159 CRISPR screens.
DR   ChiTaRS; TMEM131; human.
DR   GeneWiki; TMEM131; -.
DR   GenomeRNAi; 23505; -.
DR   Pharos; Q92545; Tdark.
DR   PRO; PR:Q92545; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q92545; Protein.
DR   Bgee; ENSG00000075568; Expressed in bronchial epithelial cell and 215 other cell types or tissues.
DR   ExpressionAtlas; Q92545; baseline and differential.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR039877; TMEM131-like.
DR   InterPro; IPR045695; TMEM131-like_conserved.
DR   InterPro; IPR022113; TMEM131-like_N.
DR   PANTHER; PTHR22050; RW1 PROTEIN HOMOLOG; 1.
DR   PANTHER; PTHR22050:SF1; TRANSMEMBRANE PROTEIN 131; 1.
DR   Pfam; PF19532; TMEM131_like; 2.
DR   Pfam; PF12371; TMEM131_like_N; 1.
DR   Genevisible; Q92545; HS.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1883
FT                   /note="Transmembrane protein 131"
FT                   /id="PRO_0000097538"
FT   TRANSMEM        1091..1111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1118..1138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1198..1580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1593..1656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1670..1712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1766..1789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1832..1858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1325
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1333..1366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1391..1421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1506..1528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1543..1557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1619..1635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1674..1712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         803
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243"
FT   MOD_RES         1322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         1863
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1871
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
SQ   SEQUENCE   1883 AA;  205138 MW;  BBC61F6C939A336E CRC64;
     MGKRAGGGAT GATTAAVSTS AGAGLEPAAA RSGGPRSAAA GLLGALHLVM TLVVAAARAE
     KEAFVQSESI IEVLRFDDGG LLQTETTLGL SSYQQKSISL YRGNCRPIRF EPPMLDFHEQ
     PVGMPKMEKV YLHNPSSEET ITLVSISATT SHFHASFFQN RKILPGGNTS FDVVFLARVV
     GNVENTLFIN TSNHGVFTYQ VFGVGVPNPY RLRPFLGARV PVNSSFSPII NIHNPHSEPL
     QVVEMYSSGG DLHLELPTGQ QGGTRKLWEI PPYETKGVMR ASFSSREADN HTAFIRIKTN
     ASDSTEFIIL PVEVEVTTAP GIYSSTEMLD FGTLRTQDLP KVLNLHLLNS GTKDVPITSV
     RPTPQNDAIT VHFKPITLKA SESKYTKVAS ISFDASKAKK PSQFSGKITV KAKEKSYSKL
     EIPYQAEVLD GYLGFDHAAT LFHIRDSPAD PVERPIYLTN TFSFAILIHD VLLPEEAKTM
     FKVHNFSKPV LILPNESGYI FTLLFMPSTS SMHIDNNILL ITNASKFHLP VRVYTGFLDY
     FVLPPKIEER FIDFGVLSAT EASNILFAII NSNPIELAIK SWHIIGDGLS IELVAVERGN
     RTTIISSLPE FEKSSLSDQS SVTLASGYFA VFRVKLTAKK LEGIHDGAIQ ITTDYEILTI
     PVKAVIAVGS LTCFPKHVVL PPSFPGKIVH QSLNIMNSFS QKVKIQQIRS LSEDVRFYYK
     RLRGNKEDLE PGKKSKIANI YFDPGLQCGD HCYVGLPFLS KSEPKVQPGV AMQEDMWDAD
     WDLHQSLFKG WTGIKENSGH RLSAIFEVNT DLQKNIISKI TAELSWPSIL SSPRHLKFPL
     TNTNCSSEEE ITLENPADVP VYVQFIPLAL YSNPSVFVDK LVSRFNLSKV AKIDLRTLEF
     QVFRNSAHPL QSSTGFMEGL SRHLILNLIL KPGEKKSVKV KFTPVHNRTV SSLIIVRNNL
     TVMDAVMVQG QGTTENLRVA GKLPGPGSSL RFKITEALLK DCTDSLKLRE PNFTLKRTFK
     VENTGQLQIH IETIEISGYS CEGYGFKVVN CQEFTLSANA SRDIIILFTP DFTASRVIRE
     LKFITTSGSE FVFILNASLP YHMLATCAEA LPRPNWELAL YIIISGIMSA LFLLVIGTAY
     LEAQGIWEPF RRRLSFEASN PPFDVGRPFD LRRIVGISSE GNLNTLSCDP GHSRGFCGAG
     GSSSRPSAGS HKQCGPSVHP HSSHSNRNSA DVENVRAKNS SSTSSRTSAQ AASSQSANKT
     SPLVLDSNTV TQGHTAGRKS KGAKQSQHGS QHHAHSPLEQ HPQPPLPPPV PQPQEPQPER
     LSPAPLAHPS HPERASSARH SSEDSDITSL IEAMDKDFDH HDSPALEVFT EQPPSPLPKS
     KGKGKPLQRK VKPPKKQEEK EKKGKGKPQE DELKDSLADD DSSSTTTETS NPDTEPLLKE
     DTEKQKGKQA MPEKHESEMS QVKQKSKKLL NIKKEIPTDV KPSSLELPYT PPLESKQRRN
     LPSKIPLPTA MTSGSKSRNA QKTKGTSKLV DNRPPALAKF LPNSQELGNT SSSEGEKDSP
     PPEWDSVPVH KPGSSTDSLY KLSLQTLNAD IFLKQRQTSP TPASPSPPAA PCPFVARGSY
     SSIVNSSSSS DPKIKQPNGS KHKLTKAASL PGKNGNPTFA AVTAGYDKSP GGNGFAKVSS
     NKTGFSSSLG ISHAPVDSDG SDSSGLWSPV SNPSSPDFTP LNSFSAFGNS FNLTGEVFSK
     LGLSRSCNQA SQRSWNEFNS GPSYLWESPA TDPSPSWPAS SGSPTHTATS VLGNTSGLWS
     TTPFSSSIWS SNLSSALPFT TPANTLASIG LMGTENSPAP HAPSTSSPAD DLGQTYNPWR
     IWSPTIGRRS SDPWSNSHFP HEN
//