ID   TM237_BOVIN             Reviewed;         400 AA.
AC   E1BN97; Q29RJ8;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Transmembrane protein 237;
GN   Name=TMEM237;
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 GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the transition zone in primary cilia. Required
CC       for ciliogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex).
CC       Interacts with TMEM107. {ECO:0000250|UniProtKB:Q96Q45}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Cell projection, cilium {ECO:0000250}.
CC       Note=Localizes at the proximal region of primary cilia were observed,
CC       consistent with localization to the transition zone. Anchored to the
CC       transition zone by RPGRIP1L (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=E1BN97-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=E1BN97-2; Sequence=VSP_042404, VSP_042405;
CC   -!- SIMILARITY: Belongs to the TMEM237 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFC03033006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03033172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC114141; AAI14142.1; -; mRNA.
DR   RefSeq; NP_001039665.1; NM_001046200.2. [E1BN97-1]
DR   AlphaFoldDB; E1BN97; -.
DR   STRING; 9913.ENSBTAP00000023181; -.
DR   PaxDb; E1BN97; -.
DR   PRIDE; E1BN97; -.
DR   GeneID; 515467; -.
DR   KEGG; bta:515467; -.
DR   CTD; 65062; -.
DR   eggNOG; ENOG502QTW0; Eukaryota.
DR   HOGENOM; CLU_061097_0_0_1; -.
DR   InParanoid; E1BN97; -.
DR   OrthoDB; 1428687at2759; -.
DR   TreeFam; TF329703; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR029409; TMEM237.
DR   PANTHER; PTHR28388; PTHR28388; 1.
DR   Pfam; PF15383; TMEM237; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..400
FT                   /note="Transmembrane protein 237"
FT                   /id="PRO_0000415829"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q45"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q45"
FT   VAR_SEQ         1
FT                   /note="M -> MTHCACARGSEAAGCELPAPGSRQPPESQALDAM (in isoform
FT                   2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042404"
FT   VAR_SEQ         17..20
FT                   /note="SAIQ -> R (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042405"
SQ   SEQUENCE   400 AA;  44562 MW;  4A5A37CA7BB5D608 CRC64;
     MGKKQVRPPR ALPPVPSAIQ DDIPLSRPKK KKPRTKTPLA SASSEGLVQT AVHRPPEGSE
     PPTKDSIEHQ EAPVQRRQKK TRLPLELETT LTQKKTASPS LLPNENGINV EPDEEPVIQK
     PRRKTKKTQP AELHYANELG VEDEDIITDE QSSPEQQSVF TAPTGISQPV GKVFVEKSRR
     FQAADRAELI KTTEKIDVSM DMKPSWTTRD VALSVHRAFR MIGVFSHGFL AGCAVWNIVV
     IYVLAGDELS DLSNLLQQYK TLAYPFQSLL YLLLALSTVS AFDRIDFAKT SVAIRNFLAL
     DPRALASFLY FTALVLSLSQ QMTSDRIHLY TPSSVNGSLW AEGIEEQVLQ PWIVVNLVVA
     VLVGLSWLFL SYRPGMDLSE ELMFSSDVEE YPDKGIKVSS