IGS21_MOUSE
ID IGS21_MOUSE Reviewed; 468 AA.
AC Q7TNR6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Immunoglobulin superfamily member 21;
DE Short=IgSF21;
DE Flags: Precursor;
GN Name=Igsf21;
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=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 [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP NRXN2, DOMAIN, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28864826; DOI=10.1038/s41467-017-00333-w;
RA Tanabe Y., Naito Y., Vasuta C., Lee A.K., Soumounou Y., Linhoff M.W.,
RA Takahashi H.;
RT "IgSF21 promotes differentiation of inhibitory synapses via binding to
RT neurexin2alpha.";
RL Nat. Commun. 8:408-408(2017).
CC -!- FUNCTION: Involved in synaptic inhibition in the brain. Selectively
CC regulates inhibitory presynaptic differentiation through interacting
CC with presynaptic NRXN2. {ECO:0000269|PubMed:28864826}.
CC -!- SUBUNIT: Interacts (Ig-like 1 domain) with NRXN2 (via Laminin G-like 1
CC domain) in a trans-interaction manner. {ECO:0000269|PubMed:28864826}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:28864826}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:28864826}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein levels)
CC (PubMed:28864826). Highly expressed in the pyramidal cell layer of the
CC dorsal and ventral hippocampal CA1 and CA3 regions, layers 5 and 6 of
CC the cortex, the thalamus and the pons and weakly expressed in the
CC cerebellum (PubMed:28864826). Expressed in neurons but not in glia
CC (PubMed:28864826). {ECO:0000269|PubMed:28864826}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the brain at both embryonic and
CC postnatal stages including the adult stage. The period of highest
CC expression of the long isoform is at around two postnatal weeks,
CC coinciding with the peak period of synaptogenesis.
CC {ECO:0000269|PubMed:28864826}.
CC -!- DOMAIN: Ig-like 1 domain is indispensable for synaptogenic activity
CC whereas Ig-like 2 domain is secondarily responsible for the activity.
CC {ECO:0000269|PubMed:28864826}.
CC -!- DISRUPTION PHENOTYPE: Mutants grow normally. They show an impaired
CC sensorimotor gating with no effect on motor activity and coordination.
CC {ECO:0000269|PubMed:28864826}.
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DR EMBL; BC055811; AAH55811.1; -; mRNA.
DR CCDS; CCDS18851.1; -.
DR RefSeq; NP_941012.1; NM_198610.2.
DR AlphaFoldDB; Q7TNR6; -.
DR IntAct; Q7TNR6; 2.
DR MINT; Q7TNR6; -.
DR STRING; 10090.ENSMUSP00000046558; -.
DR GlyConnect; 2382; 6 N-Linked glycans (1 site).
DR GlyGen; Q7TNR6; 3 sites, 6 N-linked glycans (1 site).
DR PhosphoSitePlus; Q7TNR6; -.
DR MaxQB; Q7TNR6; -.
DR PaxDb; Q7TNR6; -.
DR PeptideAtlas; Q7TNR6; -.
DR PRIDE; Q7TNR6; -.
DR ProteomicsDB; 269544; -.
DR Antibodypedia; 29423; 82 antibodies from 19 providers.
DR DNASU; 230868; -.
DR Ensembl; ENSMUST00000039331; ENSMUSP00000046558; ENSMUSG00000040972.
DR GeneID; 230868; -.
DR KEGG; mmu:230868; -.
DR UCSC; uc008vmu.2; mouse.
DR CTD; 84966; -.
DR MGI; MGI:2681842; Igsf21.
DR VEuPathDB; HostDB:ENSMUSG00000040972; -.
DR eggNOG; ENOG502QQMY; Eukaryota.
DR GeneTree; ENSGT00390000002421; -.
DR HOGENOM; CLU_054054_0_0_1; -.
DR InParanoid; Q7TNR6; -.
DR OMA; RPYTEHP; -.
DR OrthoDB; 422073at2759; -.
DR PhylomeDB; Q7TNR6; -.
DR TreeFam; TF331223; -.
DR BioGRID-ORCS; 230868; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Igsf21; mouse.
DR PRO; PR:Q7TNR6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TNR6; protein.
DR Bgee; ENSMUSG00000040972; Expressed in medial dorsal nucleus of thalamus and 130 other tissues.
DR Genevisible; Q7TNR6; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0060077; C:inhibitory synapse; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0060074; P:synapse maturation; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Signal; Synapse.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..468
FT /note="Immunoglobulin superfamily member 21"
FT /id="PRO_0000223339"
FT DOMAIN 25..132
FT /note="Ig-like 1"
FT DOMAIN 344..429
FT /note="Ig-like 2"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 468 AA; 51937 MW; B9577B5E9B66633D CRC64;
MQAAPSLRRA SCLLLAAILD LARGYLTVNI EPLPPVVAGD AVTLKCNFKT DGRMREIVWY
RVTDGGTIKQ KIFTFDAMFS TNYSHMENYR KREDLVYQST VRLPEVRISD NGPYECHVGI
YDRATREKVV LASGNIFLNV MAPPTSIEVV AADSPAPFSR YQAQNFTLVC IVSGGKPAPM
VYFKRDGEPI DAVPLTELPA ASSGPVQDSR PFRSLLHRDV DDTKMQKSLS LLDTEYRAGR
PYTERPARSL TQDPSLFVQP TTENIPETVV SREFPRWVHS AEPVYFLRHS RTPGSDGTVE
VRALLTWTLN PQIDNEALFS CEVKHPALSM PMQAEVTLVA PKGPKIMMTP SRARVGDTVR
ILVHGFQNEV FPEPMFTWTR VGSRLLDGSA EFDGKELVLE RVPAELNGSM YRCTAQNPLG
STDTHTRLIV FENPNIPRGT EDSRGSASGP AGVRLTLVLA LTVILELT
