TM201_CAEEL
ID TM201_CAEEL Reviewed; 588 AA.
AC Q22747;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transmembrane protein 201 homolog {ECO:0000305};
DE AltName: Full=Spindle-associated membrane protein homolog {ECO:0000312|WormBase:T24F1.2};
GN Name=samp-1 {ECO:0000312|WormBase:T24F1.2};
GN ORFNames=T24F1.2 {ECO:0000312|WormBase:T24F1.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25057012; DOI=10.1091/mbc.e14-05-0971;
RA Bone C.R., Tapley E.C., Gorjanacz M., Starr D.A.;
RT "The Caenorhabditis elegans SUN protein UNC-84 interacts with lamin to
RT transfer forces from the cytoplasm to the nucleoskeleton during nuclear
RT migration.";
RL Mol. Biol. Cell 25:2853-2865(2014).
CC -!- FUNCTION: Plays a role in nuclear migration in hypodermal cells.
CC {ECO:0000269|PubMed:25057012}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:25057012}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localization at the nuclear envelope does not
CC require lmn-1. {ECO:0000269|PubMed:25057012}.
CC -!- DEVELOPMENTAL STAGE: Expressed in pre-comma stage embryos, and in
CC particular in hyp7 hypodermal precursor cells.
CC {ECO:0000269|PubMed:25057012}.
CC -!- DISRUPTION PHENOTYPE: Nuclear migration defects in hyp7 hypodermal
CC precursor cells. {ECO:0000269|PubMed:25057012}.
CC -!- SIMILARITY: Belongs to the TMEM201 family. {ECO:0000305}.
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DR EMBL; BX284602; CAA90140.1; -; Genomic_DNA.
DR PIR; T25248; T25248.
DR RefSeq; NP_496416.1; NM_064015.4.
DR AlphaFoldDB; Q22747; -.
DR SMR; Q22747; -.
DR DIP; DIP-24366N; -.
DR IntAct; Q22747; 6.
DR STRING; 6239.T24F1.2; -.
DR EPD; Q22747; -.
DR PaxDb; Q22747; -.
DR PeptideAtlas; Q22747; -.
DR EnsemblMetazoa; T24F1.2.1; T24F1.2.1; WBGene00011994.
DR GeneID; 174727; -.
DR KEGG; cel:CELE_T24F1.2; -.
DR UCSC; T24F1.2; c. elegans.
DR CTD; 174727; -.
DR WormBase; T24F1.2; CE02362; WBGene00011994; samp-1.
DR eggNOG; KOG4623; Eukaryota.
DR HOGENOM; CLU_493674_0_0_1; -.
DR InParanoid; Q22747; -.
DR OMA; NKFEPRN; -.
DR OrthoDB; 898700at2759; -.
DR PRO; PR:Q22747; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011994; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
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:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:WormBase.
DR InterPro; IPR018617; Ima1_N.
DR InterPro; IPR040041; TMEM201.
DR PANTHER; PTHR28646; PTHR28646; 1.
DR Pfam; PF09779; Ima1_N; 1.
PE 2: Evidence at transcript level;
KW Membrane; Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..588
FT /note="Transmembrane protein 201 homolog"
FT /id="PRO_0000445490"
FT TOPO_DOM 1..212
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..254
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..280
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..309
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..564
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..588
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT REGION 378..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 66322 MW; 1558D1770909ADF4 CRC64;
MEVAAAVGVI ASVPILYKAI RPRIKTSVEC WFCRKSTKVE YQQRNSFTCP SCEQYNGFTE
DGDYNRRIPG QAWTTPKRYC EPGKMQSEKP STFLDRFGGV NMSPKASNGL CSECNLGQEI
IMNKVAEFEP IDEDRWNEEL EDYRYKLERM YQLCPRCTIQ VHGKLEEDKK KYSYLLKVKY
KLKHAIGSTL REVMNNQKRS RRFFFAGGST CEALHFGCLI SSIILFLANI DFLQQDAGAS
LINLPKALQD ILPEVYKYSF VINFLIFTTH LIAAFNNKCR VTLPDLLLPI LLILAMLTVL
TSSDNLSQDV ALVRGACASF STILSMAVTL LPRKKLHKKR PNKIVSSAFS VASTPISQCS
SQNSRNASLL DHDHTILRRS PHTPSASPPA MNSSPPLLRE ITNGPVWSAM RSRENKENMQ
SYQTKPNNHV ESMDWDDSES MAAQSVAQST RSSHFKPGLL SRNINERMTA QQLTPSVANL
NLDTRSVDSP SIFSRQHRQM AQQQNHTPTR SLFGPPRSMV ASQYDRSHYM APEAHTRPGS
VFTSVSQQDG HSTVSGAWQC RVIGILFALV FIVLIMQIGL FYVLFTRN
