TM87A_HUMAN
ID TM87A_HUMAN Reviewed; 555 AA.
AC Q8NBN3; Q6NT77; Q8NCA4; Q9BS46; Q9P103; Q9Y3Y7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transmembrane protein 87A {ECO:0000305};
DE Flags: Precursor;
GN Name=TMEM87A {ECO:0000312|HGNC:HGNC:24522};
GN ORFNames=PSEC0094 {ECO:0000312|EMBL:BAC11598.1};
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).
RA Luo W.Q., Chen J.H., Huang X.W., Zhou Y., Zhou H.J., Hu S.N., Yuan J.G.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, and Urinary bladder;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 424-555.
RC TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157 AND ASN-160.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, 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 [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26157166; DOI=10.1091/mbc.e14-11-1568;
RA Hirata T., Fujita M., Nakamura S., Gotoh K., Motooka D., Murakami Y.,
RA Maeda Y., Kinoshita T.;
RT "Post-Golgi anterograde transport requires GARP-dependent endosome-to-TGN
RT retrograde transport.";
RL Mol. Biol. Cell 26:3071-3084(2015).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May be involved in retrograde transport from endosomes to the
CC trans-Golgi network (TGN). {ECO:0000269|PubMed:26157166}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:26157166}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NBN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBN3-2; Sequence=VSP_022208, VSP_022209;
CC Name=3;
CC IsoId=Q8NBN3-3; Sequence=VSP_022207;
CC -!- SIMILARITY: Belongs to the LU7TM family. TMEM87 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11598.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF132733; AAF66444.1; -; mRNA.
DR EMBL; AK074870; BAC11256.1; -; mRNA.
DR EMBL; AK075403; BAC11598.1; ALT_INIT; mRNA.
DR EMBL; BC005335; AAH05335.1; -; mRNA.
DR EMBL; BC069240; AAH69240.1; -; mRNA.
DR EMBL; AL049944; CAB43218.1; -; mRNA.
DR CCDS; CCDS32205.1; -. [Q8NBN3-1]
DR CCDS; CCDS45243.1; -. [Q8NBN3-2]
DR CCDS; CCDS66742.1; -. [Q8NBN3-3]
DR PIR; T08676; T08676.
DR RefSeq; NP_001103973.1; NM_001110503.2. [Q8NBN3-2]
DR RefSeq; NP_001273416.1; NM_001286487.1. [Q8NBN3-3]
DR RefSeq; NP_056312.2; NM_015497.4. [Q8NBN3-1]
DR AlphaFoldDB; Q8NBN3; -.
DR BioGRID; 117453; 243.
DR IntAct; Q8NBN3; 29.
DR MINT; Q8NBN3; -.
DR STRING; 9606.ENSP00000374484; -.
DR GlyConnect; 1854; 19 N-Linked glycans (2 sites).
DR GlyGen; Q8NBN3; 5 sites, 21 N-linked glycans (2 sites).
DR iPTMnet; Q8NBN3; -.
DR MetOSite; Q8NBN3; -.
DR PhosphoSitePlus; Q8NBN3; -.
DR SwissPalm; Q8NBN3; -.
DR BioMuta; TMEM87A; -.
DR DMDM; 126302609; -.
DR EPD; Q8NBN3; -.
DR jPOST; Q8NBN3; -.
DR MassIVE; Q8NBN3; -.
DR MaxQB; Q8NBN3; -.
DR PaxDb; Q8NBN3; -.
DR PeptideAtlas; Q8NBN3; -.
DR PRIDE; Q8NBN3; -.
DR ProteomicsDB; 72799; -. [Q8NBN3-1]
DR ProteomicsDB; 72800; -. [Q8NBN3-2]
DR ProteomicsDB; 72801; -. [Q8NBN3-3]
DR Antibodypedia; 10648; 59 antibodies from 14 providers.
DR DNASU; 25963; -.
DR Ensembl; ENST00000307216.10; ENSP00000305894.6; ENSG00000103978.16. [Q8NBN3-2]
DR Ensembl; ENST00000389834.9; ENSP00000374484.4; ENSG00000103978.16. [Q8NBN3-1]
DR Ensembl; ENST00000448392.5; ENSP00000405379.1; ENSG00000103978.16. [Q8NBN3-3]
DR GeneID; 25963; -.
DR KEGG; hsa:25963; -.
DR MANE-Select; ENST00000389834.9; ENSP00000374484.4; NM_015497.5; NP_056312.2.
DR UCSC; uc001zpg.4; human. [Q8NBN3-1]
DR CTD; 25963; -.
DR DisGeNET; 25963; -.
DR GeneCards; TMEM87A; -.
DR HGNC; HGNC:24522; TMEM87A.
DR HPA; ENSG00000103978; Low tissue specificity.
DR neXtProt; NX_Q8NBN3; -.
DR OpenTargets; ENSG00000103978; -.
DR PharmGKB; PA142670739; -.
DR VEuPathDB; HostDB:ENSG00000103978; -.
DR eggNOG; KOG2568; Eukaryota.
DR GeneTree; ENSGT00940000159481; -.
DR HOGENOM; CLU_027525_0_0_1; -.
DR InParanoid; Q8NBN3; -.
DR OMA; TTIFMRF; -.
DR OrthoDB; 1448608at2759; -.
DR PhylomeDB; Q8NBN3; -.
DR TreeFam; TF314452; -.
DR PathwayCommons; Q8NBN3; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q8NBN3; -.
DR BioGRID-ORCS; 25963; 9 hits in 1087 CRISPR screens.
DR ChiTaRS; TMEM87A; human.
DR GenomeRNAi; 25963; -.
DR Pharos; Q8NBN3; Tdark.
DR PRO; PR:Q8NBN3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8NBN3; protein.
DR Bgee; ENSG00000103978; Expressed in secondary oocyte and 211 other tissues.
DR ExpressionAtlas; Q8NBN3; baseline and differential.
DR Genevisible; Q8NBN3; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IGI:UniProtKB.
DR InterPro; IPR009637; GPR107/GPR108-like.
DR PANTHER; PTHR21229; PTHR21229; 1.
DR Pfam; PF06814; Lung_7-TM_R; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..555
FT /note="Transmembrane protein 87A"
FT /id="PRO_0000270751"
FT TOPO_DOM 22..225
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..246
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..278
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..305
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..322
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 326..346
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..361
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 362..382
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 404..424
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..437
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 438..458
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 473..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VAR_SEQ 1..69
FT /note="MAAAAWLQVLPVILLLLGAHPSPLSFFSAGPATVAAADRSKWHIPIPSGKNY
FT FSFGKILFRNTTIFLKF -> MAHSDTVV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022207"
FT VAR_SEQ 169..181
FT /note="AMHEPLQTWQDAP -> IQMPFLKKHFLDC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022208"
FT VAR_SEQ 182..555
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022209"
FT CONFLICT 117..118
FT /note="KY -> NI (in Ref. 1; AAF66444)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="I -> S (in Ref. 1; AAF66444)"
FT /evidence="ECO:0000305"
FT CONFLICT 424..425
FT /note="MK -> KG (in Ref. 4; CAB43218)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="E -> V (in Ref. 4; CAB43218)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="L -> S (in Ref. 2; BAC11598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 63430 MW; 1ED560B42FA01076 CRC64;
MAAAAWLQVL PVILLLLGAH PSPLSFFSAG PATVAAADRS KWHIPIPSGK NYFSFGKILF
RNTTIFLKFD GEPCDLSLNI TWYLKSADCY NEIYNFKAEE VELYLEKLKE KRGLSGKYQT
SSKLFQNCSE LFKTQTFSGD FMHRLPLLGE KQEAKENGTN LTFIGDKTAM HEPLQTWQDA
PYIFIVHIGI SSSKESSKEN SLSNLFTMTV EVKGPYEYLT LEDYPLMIFF MVMCIVYVLF
GVLWLAWSAC YWRDLLRIQF WIGAVIFLGM LEKAVFYAEF QNIRYKGESV QGALILAELL
SAVKRSLART LVIIVSLGYG IVKPRLGVTL HKVVVAGALY LLFSGMEGVL RVTGAQTDLA
SLAFIPLAFL DTALCWWIFI SLTQTMKLLK LRRNIVKLSL YRHFTNTLIL AVAASIVFII
WTTMKFRIVT CQSDWRELWV DDAIWRLLFS MILFVIMVLW RPSANNQRFA FSPLSEEEEE
DEQKEPMLKE SFEGMKMRST KQEPNGNSKV NKAQEDDLKW VEENVPSSVT DVALPALLDS
DEERMITHFE RSKME
