VSTM5_MOUSE
ID VSTM5_MOUSE Reviewed; 199 AA.
AC Q9D806;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=V-set and transmembrane domain-containing protein 5 {ECO:0000303|PubMed:27683913};
DE Flags: Precursor;
GN Name=Vstm5 {ECO:0000303|PubMed:25826454, ECO:0000303|PubMed:27683913};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=25826454; DOI=10.1371/journal.pone.0121550;
RA Gu Z., Imai F., Kim I.J., Fujita H., Katayama K., Mori K., Yoshihara Y.,
RA Yoshida Y.;
RT "Expression of the immunoglobulin superfamily cell adhesion molecules in
RT the developing spinal cord and dorsal root ganglion.";
RL PLoS ONE 10:E0121550-E0121550(2015).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, GLYCOSYLATION, DISRUPTION PHENOTYPE, REGION, AND PHYLOGENETIC
RP ANALYSIS.
RX PubMed=27683913; DOI=10.1523/jneurosci.0541-16.2016;
RA Lee A.R., Ko K.W., Lee H., Yoon Y.S., Song M.R., Park C.S.;
RT "Putative cell adhesion membrane protein Vstm5 regulates neuronal
RT morphology and migration in the central nervous system.";
RL J. Neurosci. 36:10181-10197(2016).
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:0000269|PubMed:27683913}.
CC -!- SUBUNIT: Can homooligomerize through cis interactions within the same
CC cell membrane. {ECO:0000269|PubMed:27683913}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27683913};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC dendrite {ECO:0000269|PubMed:27683913}. Cell projection, axon
CC {ECO:0000269|PubMed:27683913}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the central nervous system
CC (CNS), with the highest expression in thalamus, hippocampus, cerebrum,
CC midbrain and spinal cord. Also highly expressed in stomach, kidney and
CC small intestine. {ECO:0000269|PubMed:27683913}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the ventral spinal cord, with strong
CC expression in a subset of motor neurons, and in a subset of sensory
CC neurons at embryonic day (E) 15.5 (PubMed:25826454). In the developing
CC brain, expressed at low levels on 11 dpc, rapidly increasing to peak at
CC postnatal day (P) 1, a period corresponding to the early stage of
CC postmitotic neuronal differentiation when neuronal morphogenesis or
CC synapse formation occurs, and then gradually decreasing
CC (PubMed:27683913). {ECO:0000269|PubMed:25826454,
CC ECO:0000269|PubMed:27683913}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:27683913}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown mice have significantly
CC lower density of dendritic filopodia and dendritic spines in embryonic
CC hippocampal neurons. Lower density of excitatory synapses and
CC significantly decreased dendritic spine to shaft ratio of F-actin in
CC the later stages of neuron development. Aberrant neuronal migration in
CC the cerebral cortex of developing mouse embryo. Neurons settle in the
CC marginal zone (MZ) closer to the pial side and the corresponding
CC percentage of neurons is decreased in the dense cortical plate (dCP),
CC reflecting the overmigration of those neurons. Neurons in the upper
CC cortical plate (UCP) result in a small but significant reduction in
CC both the number of dendrites and average dendrite length. Neurons of
CC embryonic brains show much lower levels of spines with the density of
CC mushroom spines markedly decreased. {ECO:0000269|PubMed:27683913}.
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DR EMBL; BC055786; AAH55786.1; -; mRNA.
DR EMBL; AK008621; BAB25783.1; -; mRNA.
DR CCDS; CCDS22833.1; -.
DR RefSeq; NP_081231.1; NM_026955.2.
DR AlphaFoldDB; Q9D806; -.
DR STRING; 10090.ENSMUSP00000034413; -.
DR GlyGen; Q9D806; 3 sites.
DR PhosphoSitePlus; Q9D806; -.
DR PaxDb; Q9D806; -.
DR PRIDE; Q9D806; -.
DR ProteomicsDB; 297825; -.
DR Antibodypedia; 31599; 22 antibodies from 11 providers.
DR DNASU; 69137; -.
DR Ensembl; ENSMUST00000034413; ENSMUSP00000034413; ENSMUSG00000031937.
DR GeneID; 69137; -.
DR KEGG; mmu:69137; -.
DR UCSC; uc009ofk.1; mouse.
DR CTD; 387804; -.
DR MGI; MGI:1916387; Vstm5.
DR VEuPathDB; HostDB:ENSMUSG00000031937; -.
DR eggNOG; ENOG502S0GW; Eukaryota.
DR GeneTree; ENSGT00960000186634; -.
DR HOGENOM; CLU_118644_0_0_1; -.
DR InParanoid; Q9D806; -.
DR OMA; CNRCAYK; -.
DR OrthoDB; 1260992at2759; -.
DR PhylomeDB; Q9D806; -.
DR TreeFam; TF332950; -.
DR BioGRID-ORCS; 69137; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Vstm5; mouse.
DR PRO; PR:Q9D806; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D806; protein.
DR Bgee; ENSMUSG00000031937; Expressed in lumbar dorsal root ganglion and 135 other tissues.
DR Genevisible; Q9D806; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; IMP:UniProtKB.
DR GO; GO:1904891; P:positive regulation of excitatory synapse assembly; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR024303; NK_rcpt_2B4_Ig_dom.
DR Pfam; PF11465; Receptor_2B4; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein 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_0000340694"
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 35..138
FT /note="Ig-like C2-type"
FT REGION 169..185
FT /note="Important for CDC42-dependent filopodia induction"
FT /evidence="ECO:0000269|PubMed:27683913"
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; 22564 MW; 77400D2FF9AD4642 CRC64;
MRPLRCGERT QGIPLGLLAF WVTAARCLQS QGVSLYIPQS AINATVQQDI LLSVDYICHG
VPTIEWKYTP NWGVQRIVEW KPGTPANVSQ SHRDRVCTFD NGSIQLFNVS VKDSGYYIVT
VTEHPGSSQS GTILLRVSEI RYEDLHFVAV FFALLAAVAV VLISLMWVCN QCAYKFQRKR
RYKLKESTTE EIEMKEVEC
