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 18-JAN-2017, entry version 74.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the 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
RT project: 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
RT 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.,
RA Koch B., Mattaj I.W., Gomes E.R.;
RT "Samp1 is a component of TAN lines and is required for nuclear
RT movement.";
RL J. Cell Sci. 125:1099-1105(2012).
CC -!- FUNCTION: Involved in nuclear movement during fibroblast
CC polarization and migration (PubMed:22349700). May recruit Ran
CC GTPase to the nuclear periphery (By similarity).
CC {ECO:0000250|UniProtKB:Q5SNT2, 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
CC the 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
CC and 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
CC GTPase; has a greater affinity for Ran-GTP over Ran-GDP (By
CC similarity). {ECO:0000250|UniProtKB:Q5SNT2,
CC ECO:0000269|PubMed:22349700}.
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
CC is located on the nucleoplasmic side. During interphase, isoform 2
CC is distributed in the inner nuclear membrane and during mitosis,
CC it is found in the ER but it also localizes to the polar regions
CC of the mitotic spindle (By similarity).
CC {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;
DR EMBL; AK079157; BAC37562.1; -; mRNA.
DR EMBL; AK153631; BAE32126.1; -; mRNA.
DR EMBL; AL626808; CAM22693.1; -; Genomic_DNA.
DR EMBL; AL626808; CAM22694.1; -; Genomic_DNA.
DR EMBL; AL626808; CAP19192.1; -; 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 UniGene; Mm.266704; -.
DR ProteinModelPortal; A2A8U2; -.
DR IntAct; A2A8U2; 1.
DR MINT; MINT-4111729; -.
DR STRING; 10090.ENSMUSP00000050481; -.
DR iPTMnet; A2A8U2; -.
DR PhosphoSitePlus; A2A8U2; -.
DR MaxQB; A2A8U2; -.
DR PaxDb; A2A8U2; -.
DR PeptideAtlas; A2A8U2; -.
DR PRIDE; A2A8U2; -.
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 eggNOG; KOG4623; Eukaryota.
DR eggNOG; ENOG41123RR; LUCA.
DR GeneTree; ENSGT00390000002713; -.
DR HOGENOM; HOG000154619; -.
DR HOVERGEN; HBG057857; -.
DR InParanoid; A2A8U2; -.
DR OMA; EAWAFGQ; -.
DR OrthoDB; EOG091G07TP; -.
DR PhylomeDB; A2A8U2; -.
DR TreeFam; TF106107; -.
DR ChiTaRS; Tmem201; mouse.
DR PRO; PR:A2A8U2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR Bgee; ENSMUSG00000044700; -.
DR CleanEx; MM_TMEM201; -.
DR Genevisible; A2A8U2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0005521; F:lamin binding; IDA:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR GO; GO:0030473; P:nuclear migration along microtubule; IBA:GO_Central.
DR InterPro; IPR018861; DUF2448.
DR InterPro; IPR018617; Ima1_N.
DR Pfam; PF10476; DUF2448; 1.
DR Pfam; PF09779; Ima1_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 664 Transmembrane protein 201.
FT /FTId=PRO_0000317199.
FT TOPO_DOM 1 214 Nuclear. {ECO:0000250|UniProtKB:Q5SNT2}.
FT TRANSMEM 215 235 Helical. {ECO:0000255}.
FT TOPO_DOM 236 297 Perinuclear space. {ECO:0000305}.
FT TRANSMEM 298 318 Helical. {ECO:0000255}.
FT TOPO_DOM 319 322 Nuclear. {ECO:0000305}.
FT TRANSMEM 323 343 Helical. {ECO:0000255}.
FT TOPO_DOM 344 356 Perinuclear space. {ECO:0000305}.
FT TRANSMEM 357 374 Helical. {ECO:0000255}.
FT TOPO_DOM 375 642 Nuclear. {ECO:0000250|UniProtKB:Q5SNT2,
FT ECO:0000305}.
FT TRANSMEM 643 663 Helical. {ECO:0000255}.
FT TOPO_DOM 664 664 Perinuclear space. {ECO:0000305}.
FT COMPBIAS 390 520 Ser-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 441 441 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 444 444 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 450 450 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 454 454 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 466 466 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 477 477 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 480 480 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT MOD_RES 529 529 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q5SNT2}.
FT VAR_SEQ 388 392 YFSGD -> SEKQQ (in isoform 2).
FT {ECO:0000305}.
FT /FTId=VSP_030917.
FT VAR_SEQ 393 664 Missing (in isoform 2). {ECO:0000305}.
FT /FTId=VSP_030918.
FT VAR_SEQ 633 634 AR -> GL (in isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_030919.
FT VAR_SEQ 635 664 Missing (in isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_030920.
FT CONFLICT 128 128 Q -> H (in Ref. 1; BAC37562).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 191 389 ipfam:DUF2448 [T]
FT MYHIT 46 171 ipfam:Ima1_N [T]
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
//
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