TM201_MOUSE
ID TM201_MOUSE Reviewed; 664 AA.
AC A2A8U2; Q3U5F3; Q6GQS9; Q8BNY3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transmembrane protein 201;
DE AltName: Full=Spindle-associated membrane protein 1;
GN Name=Tmem201; Synonyms=D4Ertd429e, Net5, Samp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SUN2 AND LMNA.
RX PubMed=22349700; DOI=10.1242/jcs.087049;
RA Borrego-Pinto J., Jegou T., Osorio D.S., Aurade F., Gorjanacz M., Koch B.,
RA Mattaj I.W., Gomes E.R.;
RT "Samp1 is a component of TAN lines and is required for nuclear movement.";
RL J. Cell Sci. 125:1099-1105(2012).
CC -!- FUNCTION: Involved in nuclear movement during fibroblast polarization
CC and migration (PubMed:22349700). May recruit Ran GTPase to the nuclear
CC periphery (By similarity). {ECO:0000250|UniProtKB:Q5SNT2,
CC ECO:0000269|PubMed:22349700}.
CC -!- FUNCTION: [Isoform 2]: May define a distinct membrane domain in the
CC vicinity of the mitotic spindle. Involved in the organization of the
CC nuclear envelope implicating EMD, SUN1 and A-type lamina.
CC {ECO:0000250|UniProtKB:Q5SNT2}.
CC -!- FUNCTION: [Isoform 3]: Proposed to be involved in actin-dependent
CC nuclear movement; via SUN2 associates with transmembrane actin-
CC associated nuclear (TAN) lines which are bound to F-actin cables and
CC couple the nucleus to retrograde actin flow.
CC {ECO:0000305|PubMed:22349700}.
CC -!- SUBUNIT: Isoform 2 interacts with EMD (By similarity). Isoform 3
CC interacts with SUN2 and LMNA (PubMed:22349700). May bind to Ran GTPase;
CC has a greater affinity for Ran-GTP over Ran-GDP (By similarity).
CC {ECO:0000250|UniProtKB:Q5SNT2, ECO:0000269|PubMed:22349700}.
CC -!- INTERACTION:
CC A2A8U2-3; Q8BJS4: Sun2; NbExp=3; IntAct=EBI-12591474, EBI-646914;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5SNT2}. Note=The C-terminal of isoform 2 is
CC located on the nucleoplasmic side. During interphase, isoform 2 is
CC distributed in the inner nuclear membrane and during mitosis, it is
CC found in the ER but it also localizes to the polar regions of the
CC mitotic spindle (By similarity). {ECO:0000250|UniProtKB:Q5SNT2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Samp1c;
CC IsoId=A2A8U2-1; Sequence=Displayed;
CC Name=2; Synonyms=Samp1, Samp1a;
CC IsoId=A2A8U2-2; Sequence=VSP_030917, VSP_030918;
CC Name=3; Synonyms=Samp1b;
CC IsoId=A2A8U2-3; Sequence=VSP_030919, VSP_030920;
CC -!- SIMILARITY: Belongs to the TMEM201 family. {ECO:0000305}.
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DR EMBL; AK079157; BAC37562.1; -; mRNA.
DR EMBL; AK153631; BAE32126.1; -; mRNA.
DR EMBL; AL626808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072645; AAH72645.1; -; mRNA.
DR CCDS; CCDS18965.1; -. [A2A8U2-2]
DR CCDS; CCDS71523.1; -. [A2A8U2-1]
DR RefSeq; NP_001271199.1; NM_001284270.1. [A2A8U2-1]
DR RefSeq; NP_001271202.1; NM_001284273.1.
DR RefSeq; NP_808340.2; NM_177672.4. [A2A8U2-2]
DR AlphaFoldDB; A2A8U2; -.
DR BioGRID; 231056; 2.
DR IntAct; A2A8U2; 3.
DR STRING; 10090.ENSMUSP00000050481; -.
DR iPTMnet; A2A8U2; -.
DR PhosphoSitePlus; A2A8U2; -.
DR EPD; A2A8U2; -.
DR jPOST; A2A8U2; -.
DR MaxQB; A2A8U2; -.
DR PaxDb; A2A8U2; -.
DR PeptideAtlas; A2A8U2; -.
DR PRIDE; A2A8U2; -.
DR ProteomicsDB; 259547; -. [A2A8U2-1]
DR ProteomicsDB; 259548; -. [A2A8U2-2]
DR ProteomicsDB; 259549; -. [A2A8U2-3]
DR Antibodypedia; 62878; 21 antibodies from 8 providers.
DR DNASU; 230917; -.
DR Ensembl; ENSMUST00000054459; ENSMUSP00000050481; ENSMUSG00000044700. [A2A8U2-3]
DR Ensembl; ENSMUST00000103208; ENSMUSP00000099497; ENSMUSG00000044700. [A2A8U2-2]
DR Ensembl; ENSMUST00000105687; ENSMUSP00000101312; ENSMUSG00000044700. [A2A8U2-1]
DR GeneID; 230917; -.
DR KEGG; mmu:230917; -.
DR UCSC; uc008vwz.2; mouse. [A2A8U2-1]
DR UCSC; uc008vxa.3; mouse. [A2A8U2-3]
DR UCSC; uc008vxc.2; mouse. [A2A8U2-2]
DR CTD; 199953; -.
DR MGI; MGI:1196277; Tmem201.
DR VEuPathDB; HostDB:ENSMUSG00000044700; -.
DR eggNOG; KOG4623; Eukaryota.
DR GeneTree; ENSGT00390000002713; -.
DR HOGENOM; CLU_479766_0_0_1; -.
DR InParanoid; A2A8U2; -.
DR OMA; LWFFILC; -.
DR PhylomeDB; A2A8U2; -.
DR TreeFam; TF106107; -.
DR BioGRID-ORCS; 230917; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Tmem201; mouse.
DR PRO; PR:A2A8U2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A8U2; protein.
DR Bgee; ENSMUSG00000044700; Expressed in secondary oocyte and 224 other tissues.
DR Genevisible; A2A8U2; MM.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0005521; F:lamin binding; IDA:MGI.
DR GO; GO:0051642; P:centrosome localization; ISO:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0006998; P:nuclear envelope organization; ISO:MGI.
DR GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR GO; GO:0030473; P:nuclear migration along microtubule; IBA:GO_Central.
DR GO; GO:0090435; P:protein localization to nuclear envelope; ISO:MGI.
DR InterPro; IPR018617; Ima1_N.
DR InterPro; IPR040041; TMEM201.
DR InterPro; IPR018861; TMEM201_C.
DR PANTHER; PTHR28646; PTHR28646; 1.
DR Pfam; PF10476; DUF2448; 1.
DR Pfam; PF09779; Ima1_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..664
FT /note="Transmembrane protein 201"
FT /id="PRO_0000317199"
FT TOPO_DOM 1..214
FT /note="Nuclear"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..297
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..322
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..356
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 357..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..642
FT /note="Nuclear"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2, ECO:0000305"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT REGION 245..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT VAR_SEQ 388..392
FT /note="YFSGD -> SEKQQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030917"
FT VAR_SEQ 393..664
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030918"
FT VAR_SEQ 633..634
FT /note="AR -> GL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030919"
FT VAR_SEQ 635..664
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030920"
FT CONFLICT 128
FT /note="Q -> H (in Ref. 1; BAC37562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 72500 MW; FF1207C8C15B33C2 CRC64;
MEGVSALLAS CPTAGLAGGL GVTACAAAGV VLYRIARRVK PTHTMVNCWF CNHDTLVPYG
NRNCWDCPHC EQYNGFQENG DYNKPIPAQY MEHLNHVVSS VPSPRDPAQP QQWVSSQVLL
CRRCSHHQTT KIKQLAAFTP REEGRYDEEI EVYRHHLEQM YKLCRPCQAA VEYYIKHQNR
QLRALLLSHQ FRRREADQAH GQSFSSSAVK APFQVILLRA LAFLACAFLL FTTLYGPSEP
FTPGAALPPA LPPGGNSSAA SDNTTSQAEG WQQLLGLLPE HATEKLHEAW AFGQSHQTSI
VAVGLLTCLL AMLLAGRIRL RRIDAFSTCL WALLLGLHLA EHYLQAASPG WLDTLKFSTT
SLCCLVGFTA AVATRKSTGP RRFRPRRYFS GDSASLFPSS PSLAVPYPSV TSSPASLFIP
TPPGFLPLTK QQLFRSPRRV SPSSLPGRLS RALSLGTIPP LTRTDSGYLF SGSRPPSRVS
PAGEVSLSDY FSLLSSSFPA SPLPSPAPSV ASSVASSSGS LRHRRPLISP ARLNLKGQKL
LLFSSPGEAP NTPSSSEEFS PPNGSLFIES PQLPQRNHTR DTKHTMEMRS MLARDSARSS
HSIKKEDESS QSSTCVVDTT TKGCSEETTP WKARVSPSLV RGLLAVSLAV NALFTSAYLY
QSLR
