ID   TM201_BOVIN             Reviewed;         393 AA.
AC   Q32PF0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Transmembrane protein 201;
GN   Name=TMEM201;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May define a distinct membrane domain in the vicinity of the
CC       mitotic spindle. Involved in the organization of the nuclear envelope
CC       implicating EMD, SUN1 and A-type lamina. Involved in nuclear movement
CC       during fibroblast polarization and migration. Proposed to be involved
CC       in actin-dependent nuclear movement via association with transmembrane
CC       actin-associated nuclear (TAN) lines which are bound to F-actin cables
CC       and couple the nucleus to retrograde actin flow. May recruit Ran GTPase
CC       to the nuclear periphery. {ECO:0000250|UniProtKB:A2A8U2,
CC       ECO:0000250|UniProtKB:Q5SNT2}.
CC   -!- SUBUNIT: Interacts with EMD. Interacts with SUN2 and LMNA. May bind to
CC       Ran GTPase; has a greater affinity for Ran-GTP over Ran-GDP.
CC       {ECO:0000250|UniProtKB:A2A8U2, ECO:0000250|UniProtKB:Q5SNT2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC       {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein
CC       {ECO:0000305}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q5SNT2}.
CC   -!- SIMILARITY: Belongs to the TMEM201 family. {ECO:0000305}.
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DR   EMBL; BC108140; AAI08141.1; -; mRNA.
DR   RefSeq; NP_001032528.1; NM_001037451.1.
DR   AlphaFoldDB; Q32PF0; -.
DR   STRING; 9913.ENSBTAP00000004131; -.
DR   PaxDb; Q32PF0; -.
DR   GeneID; 507444; -.
DR   KEGG; bta:507444; -.
DR   CTD; 199953; -.
DR   eggNOG; KOG4623; Eukaryota.
DR   InParanoid; Q32PF0; -.
DR   OrthoDB; 532133at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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   Acetylation; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..393
FT                   /note="Transmembrane protein 201"
FT                   /id="PRO_0000317197"
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..298
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..323
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        345..357
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        358..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..393
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SNT2, ECO:0000305"
FT   REGION          246..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SNT2"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   393 AA;  43243 MW;  3149C35D3B14BD7A CRC64;
     MEGVSALLAR CPTAGLAGGL GVTACAAAGV LLYRIARRMK PTHTVVNCWF CNQDTVVPYG
     NRNCWDCPHC EQYNGFQENG DYNKPIPAQY LEHLNHVVSG SPGPRAPAQP LQWVSSQVLL
     CRRCSHHQTA KVKQLAAFSP RDEGRYDEEI EVYRHHLEQM YKLCRPCQAA VEHYIKHQNR
     QLRALLLSHQ FKRREADQTH TQSFCASAVK APAQVIVLRA LAFLACAFLL TTALYGTSNP
     FAPGAPLPPT LPTGSNGSAP PDNGTATGAE GWRQLLGLLP EHAAEKLREA WAFGQSHQMG
     VVALGLLTCL LAMLLAGRIR LRRIDAFSTG LWALLLGLHL AEQYLQAASP SWLDTLKFST
     TSLCCLVGFT AAVATRKATG PRRFRPRRSE KQQ