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LSM12_HUMAN
ID   LSM12_HUMAN             Reviewed;         195 AA.
AC   Q3MHD2; Q86YB1; Q96NL5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Protein LSM12;
GN   Name=LSM12;
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).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-128 (ISOFORM 2), AND VARIANT ARG-77.
RC   TISSUE=Brain;
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   PROTEIN SEQUENCE OF 2-18; 25-37 AND 73-86, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, 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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, 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   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MASS SPECTROMETRY, AND INTERACTION
RP   WITH TPCN2.
RX   PubMed=34362892; DOI=10.1038/s41467-021-24735-z;
RA   Zhang J., Guan X., Shah K., Yan J.;
RT   "Lsm12 is an NAADP receptor and a two-pore channel regulatory protein
RT   required for calcium mobilization from acidic organelles.";
RL   Nat. Commun. 12:4739-4739(2021).
CC   -!- FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) binding
CC       protein (PubMed:34362892). Confers NAADP sensitivity to the two pore
CC       channel complex (TPCs) by acting as TPC accessory protein necessary for
CC       NAADP-evoked Ca(2+) release (PubMed:34362892).
CC       {ECO:0000269|PubMed:34362892}.
CC   -!- SUBUNIT: Found in a complex with LSM12, TPCN1 and TPCN2
CC       (PubMed:34362892). Interacts with TPCN2 (PubMed:34362892).
CC       {ECO:0000269|PubMed:34362892}.
CC   -!- INTERACTION:
CC       Q3MHD2; Q9Y333: LSM2; NbExp=3; IntAct=EBI-725133, EBI-347416;
CC       Q3MHD2; P62310: LSM3; NbExp=3; IntAct=EBI-725133, EBI-348239;
CC       Q3MHD2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-725133, EBI-741158;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34362892}.
CC       Note=Colocalizes with TPCN2. {ECO:0000269|PubMed:34362892}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3MHD2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3MHD2-2; Sequence=VSP_028241;
CC   -!- SIMILARITY: Belongs to the LSM12 family. {ECO:0000305}.
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DR   EMBL; AK055218; BAB70877.1; -; mRNA.
DR   EMBL; AC023855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF456277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC044587; AAH44587.1; -; mRNA.
DR   EMBL; BC105288; AAI05289.1; -; mRNA.
DR   CCDS; CCDS11475.1; -. [Q3MHD2-1]
DR   RefSeq; NP_689557.1; NM_152344.3. [Q3MHD2-1]
DR   AlphaFoldDB; Q3MHD2; -.
DR   BioGRID; 125889; 136.
DR   IntAct; Q3MHD2; 31.
DR   MINT; Q3MHD2; -.
DR   STRING; 9606.ENSP00000466718; -.
DR   ChEMBL; CHEMBL4295839; -.
DR   GlyGen; Q3MHD2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3MHD2; -.
DR   PhosphoSitePlus; Q3MHD2; -.
DR   BioMuta; LSM12; -.
DR   DMDM; 158705881; -.
DR   EPD; Q3MHD2; -.
DR   jPOST; Q3MHD2; -.
DR   MassIVE; Q3MHD2; -.
DR   MaxQB; Q3MHD2; -.
DR   PaxDb; Q3MHD2; -.
DR   PeptideAtlas; Q3MHD2; -.
DR   PRIDE; Q3MHD2; -.
DR   ProteomicsDB; 61781; -. [Q3MHD2-1]
DR   ProteomicsDB; 61782; -. [Q3MHD2-2]
DR   Antibodypedia; 29665; 95 antibodies from 20 providers.
DR   DNASU; 124801; -.
DR   Ensembl; ENST00000293406.8; ENSP00000293406.3; ENSG00000161654.10. [Q3MHD2-1]
DR   Ensembl; ENST00000591247.6; ENSP00000466718.1; ENSG00000161654.10. [Q3MHD2-1]
DR   GeneID; 124801; -.
DR   KEGG; hsa:124801; -.
DR   MANE-Select; ENST00000293406.8; ENSP00000293406.3; NM_001371445.1; NP_001358374.1.
DR   UCSC; uc002iev.3; human. [Q3MHD2-1]
DR   CTD; 124801; -.
DR   DisGeNET; 124801; -.
DR   GeneCards; LSM12; -.
DR   HGNC; HGNC:26407; LSM12.
DR   HPA; ENSG00000161654; Low tissue specificity.
DR   MIM; 611793; gene.
DR   neXtProt; NX_Q3MHD2; -.
DR   OpenTargets; ENSG00000161654; -.
DR   PharmGKB; PA142671502; -.
DR   VEuPathDB; HostDB:ENSG00000161654; -.
DR   eggNOG; KOG4401; Eukaryota.
DR   GeneTree; ENSGT00390000006956; -.
DR   HOGENOM; CLU_073383_3_0_1; -.
DR   InParanoid; Q3MHD2; -.
DR   OMA; WEGANIR; -.
DR   OrthoDB; 1601482at2759; -.
DR   PhylomeDB; Q3MHD2; -.
DR   PathwayCommons; Q3MHD2; -.
DR   SignaLink; Q3MHD2; -.
DR   BioGRID-ORCS; 124801; 232 hits in 1079 CRISPR screens.
DR   ChiTaRS; LSM12; human.
DR   GenomeRNAi; 124801; -.
DR   Pharos; Q3MHD2; Tbio.
DR   PRO; PR:Q3MHD2; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q3MHD2; protein.
DR   Bgee; ENSG00000161654; Expressed in gingival epithelium and 204 other tissues.
DR   ExpressionAtlas; Q3MHD2; baseline and differential.
DR   Genevisible; Q3MHD2; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   InterPro; IPR019181; Anticodon-binding_dom.
DR   InterPro; IPR039683; Lsm12-like.
DR   PANTHER; PTHR13542; PTHR13542; 1.
DR   Pfam; PF09793; AD; 1.
DR   SMART; SM00995; AD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..195
FT                   /note="Protein LSM12"
FT                   /id="PRO_0000305126"
FT   REGION          4..67
FT                   /note="Required for NAADP and TPCN2 binding"
FT                   /evidence="ECO:0000269|PubMed:34362892"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         75
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         42
FT                   /note="K -> ISPE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028241"
FT   VARIANT         77
FT                   /note="P -> R (in dbSNP:rs17854322)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035166"
FT   VARIANT         173
FT                   /note="V -> L (in dbSNP:rs59168537)"
FT                   /id="VAR_062209"
SQ   SEQUENCE   195 AA;  21701 MW;  BCEDE62DA43D86C7 CRC64;
     MAAPPGEYFS VGSQVSCRTC QEQRLQGEVV AFDYQSKMLA LKCPSSSGKP NHADILLINL
     QYVSEVEIIN DRTETPPPLA SLNVSKLASK ARTEKEEKLS QAYAISAGVS LEGQQLFQTI
     HKTIKDCKWQ EKNIVVMEEV VITPPYQVEN CKGKEGSALS HVRKIVEKHF RDVESQKILQ
     RSQAQQPQKE AALSS
 
 
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