ID   TM201_DANRE             Reviewed;         651 AA.
AC   A4IG66;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Transmembrane protein 201;
GN   Name=tmem201; ORFNames=zgc:162289;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in actin-dependent nuclear movement. May be
CC       involved in the organization of the nuclear envelope. May recruit Ran
CC       GTPase to the nuclear periphery. {ECO:0000250|UniProtKB:A2A8U2,
CC       ECO:0000250|UniProtKB:Q5SNT2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC       {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TMEM201 family. {ECO:0000305}.
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DR   EMBL; BC134950; AAI34951.1; -; mRNA.
DR   RefSeq; NP_001103936.1; NM_001110466.1.
DR   AlphaFoldDB; A4IG66; -.
DR   STRING; 7955.ENSDARP00000099162; -.
DR   PaxDb; A4IG66; -.
DR   PeptideAtlas; A4IG66; -.
DR   GeneID; 563814; -.
DR   KEGG; dre:563814; -.
DR   CTD; 199953; -.
DR   ZFIN; ZDB-GENE-070410-61; tmem201.
DR   eggNOG; KOG4623; Eukaryota.
DR   InParanoid; A4IG66; -.
DR   OrthoDB; 532133at2759; -.
DR   PhylomeDB; A4IG66; -.
DR   PRO; PR:A4IG66; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR   GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005521; F:lamin binding; IBA:GO_Central.
DR   GO; GO:0030473; P:nuclear migration along microtubule; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..651
FT                   /note="Transmembrane protein 201"
FT                   /id="PRO_0000317200"
FT   TOPO_DOM        1..209
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..296
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..321
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..352
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..625
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SNT2, ECO:0000305"
FT   TRANSMEM        626..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        647..651
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000305"
FT   REGION          469..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   651 AA;  72016 MW;  E01639A152DC14FC CRC64;
     MEALNQILIE YPPLVVGGVG ATAVAAGGAL IYRIATRKKP THLQVNCWFC NQDTVVPYGN
     RNCWDCPYCE QYNGFQENGD YNKPIPAQYM EHLNHGVSAG VPETPKTLQW VNCQMLLCKK
     CNNNQTLKIK QLASFIPRED ENYDEEIEVY KHHLEQTYKL CRPCQTAVEY YIKHQNRQLR
     ALLFNHQLRR TRDADKAFIK NTYSLSTPAW LILLRILTFL ACAFLVAVAL SGYVDESPSV
     TQTLSGGVVP PKRVLQNENE SKTDEGSLMW DDLMGLLPEK AVENARLFWQ SGSDHQMAVA
     SVGLLTCITG VLMAGPVRLR RIDAVASVLW LLVICFYLAE CYLKTDVPSW LEMVKFGITS
     VCCLVGFAAA VATRKSTSQR RARGRRYLSG GSPGEFFCNH GPLLSAPVSE SSTFIPTPPP
     NLSQLLIRQQ SQRTRKASPS SLPGRLNRAL SLGTIPSLAR ADSGFLFSGS RPSSQCKDSP
     PSDYYSLKSG SRPSSPGPSP TPSVAGSVTS TSSSARQRRP LISPARLNIS GQKLRLFSSP
     LEPFSLASPP PFLSEHNPMH SRGFLPDVPH FHLQNHGSVI DEGSVFEHLE KPMGSSSSSS
     NCHVDTTTGN NIESKPGWKG FLGMTLWPGL LFASLTINLS FICIYVYYNW R