ID   VSTM5_RAT               Reviewed;         199 AA.
AC   Q5M7U7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=V-set and transmembrane domain-containing protein 5;
DE   Flags: Precursor;
GN   Name=Vstm5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cell adhesion-like membrane protein of the central nervous
CC       system (CNS) which modulates both the position and complexity of
CC       central neurons by altering their membrane morphology and dynamics.
CC       Involved in the formation of neuronal dendrites and protrusions
CC       including dendritic filopodia. In synaptogenesis, regulates synapse
CC       formation by altering dendritic spine morphology and actin
CC       distribution. Promotes formation of unstable neuronal spines such as
CC       thin and branched types. Regulates neuronal morphogenesis and migration
CC       during cortical development in the brain.
CC       {ECO:0000250|UniProtKB:Q9D806}.
CC   -!- SUBUNIT: Can homooligomerize through cis interactions within the same
CC       cell membrane. {ECO:0000250|UniProtKB:Q9D806}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9D806};
CC       Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC       dendrite {ECO:0000250|UniProtKB:Q9D806}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9D806}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9D806}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH88439.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC088439; AAH88439.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001138342.1; NM_001144870.1.
DR   AlphaFoldDB; Q5M7U7; -.
DR   STRING; 10116.ENSRNOP00000013927; -.
DR   GlyGen; Q5M7U7; 3 sites.
DR   PaxDb; Q5M7U7; -.
DR   Ensembl; ENSRNOT00000013927; ENSRNOP00000013927; ENSRNOG00000010480.
DR   GeneID; 500947; -.
DR   KEGG; rno:500947; -.
DR   UCSC; RGD:1563328; rat.
DR   CTD; 387804; -.
DR   RGD; 1563328; Vstm5.
DR   eggNOG; ENOG502S0GW; Eukaryota.
DR   GeneTree; ENSGT00960000186634; -.
DR   HOGENOM; CLU_118644_0_0_1; -.
DR   InParanoid; Q5M7U7; -.
DR   OMA; CNRCAYK; -.
DR   OrthoDB; 1260992at2759; -.
DR   PhylomeDB; Q5M7U7; -.
DR   TreeFam; TF332950; -.
DR   PRO; PR:Q5M7U7; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000010480; Expressed in kidney and 9 other tissues.
DR   Genevisible; Q5M7U7; RN.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR   GO; GO:1904891; P:positive regulation of excitatory synapse assembly; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0021517; P:ventral spinal cord development; ISO:RGD.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR024303; NK_rcpt_2B4_Ig_dom.
DR   Pfam; PF11465; Receptor_2B4; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Developmental protein; Glycoprotein;
KW   Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..199
FT                   /note="V-set and transmembrane domain-containing protein 5"
FT                   /id="PRO_0000340695"
FT   TOPO_DOM        28..146
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          36..138
FT                   /note="Ig-like C2-type"
FT   REGION          169..185
FT                   /note="Important for CDC42-dependent filopodia induction"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D806"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   199 AA;  22486 MW;  15D44999EBC4241F CRC64;
     MRPPRCVGRT QGIPLGLLAF WVATARCLQS QGVSLYIPRS AINATVQEDI LLSVDYICHG
     VPTIEWEYTP NWGVQKIVEW KPGTPANVSQ SHRDRVCTFD NGSIQLFSVG VRDSGYYVIT
     VTEHPGSSQS GTILLHVSEI RYEDLHFVAV FFALLAAVAV VLISLMWVCN QCAYKFQRKR
     RYKLRESTTE EIEMKDVEC