Immunoglobulin superfamily member 21 (IgSF21)

 IGS21_MOUSE             Reviewed;         468 AA.
 Q7TNR6;
 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
 01-OCT-2003, sequence version 1.
 25-MAY-2022, entry version 131.
 RecName: Full=Immunoglobulin superfamily member 21;
          Short=IgSF21;
 Flags: Precursor;
 Name=Igsf21;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
 Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=C57BL/6J; TISSUE=Brain;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [2]
 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
 NRXN2, DOMAIN, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
 PubMed=28864826; DOI=10.1038/s41467-017-00333-w;
 Tanabe Y., Naito Y., Vasuta C., Lee A.K., Soumounou Y., Linhoff M.W.,
 Takahashi H.;
 "IgSF21 promotes differentiation of inhibitory synapses via binding to
 neurexin2alpha.";
 Nat. Commun. 8:408-408(2017).
 -!- FUNCTION: Involved in synaptic inhibition in the brain. Selectively
     regulates inhibitory presynaptic differentiation through interacting
     with presynaptic NRXN2. {ECO:0000269|PubMed:28864826}.
 -!- SUBUNIT: Interacts (Ig-like 1 domain) with NRXN2 (via Laminin G-like 1
     domain) in a trans-interaction manner. {ECO:0000269|PubMed:28864826}.
 -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
     membrane {ECO:0000269|PubMed:28864826}; Lipid-anchor, GPI-anchor
     {ECO:0000269|PubMed:28864826}.
 -!- TISSUE SPECIFICITY: Expressed in brain (at protein levels)
     (PubMed:28864826). Highly expressed in the pyramidal cell layer of the
     dorsal and ventral hippocampal CA1 and CA3 regions, layers 5 and 6 of
     the cortex, the thalamus and the pons and weakly expressed in the
     cerebellum (PubMed:28864826). Expressed in neurons but not in glia
     (PubMed:28864826). {ECO:0000269|PubMed:28864826}.
 -!- DEVELOPMENTAL STAGE: Expressed in the brain at both embryonic and
     postnatal stages including the adult stage. The period of highest
     expression of the long isoform is at around two postnatal weeks,
     coinciding with the peak period of synaptogenesis.
     {ECO:0000269|PubMed:28864826}.
 -!- DOMAIN: Ig-like 1 domain is indispensable for synaptogenic activity
     whereas Ig-like 2 domain is secondarily responsible for the activity.
     {ECO:0000269|PubMed:28864826}.
 -!- DISRUPTION PHENOTYPE: Mutants grow normally. They show an impaired
     sensorimotor gating with no effect on motor activity and coordination.
     {ECO:0000269|PubMed:28864826}.
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 EMBL; BC055811; AAH55811.1; -; mRNA.
 CCDS; CCDS18851.1; -.
 RefSeq; NP_941012.1; NM_198610.2.
 AlphaFoldDB; Q7TNR6; -.
 IntAct; Q7TNR6; 2.
 MINT; Q7TNR6; -.
 STRING; 10090.ENSMUSP00000046558; -.
 GlyConnect; 2382; 6 N-Linked glycans (1 site).
 GlyGen; Q7TNR6; 3 sites, 6 N-linked glycans (1 site).
 PhosphoSitePlus; Q7TNR6; -.
 MaxQB; Q7TNR6; -.
 PaxDb; Q7TNR6; -.
 PeptideAtlas; Q7TNR6; -.
 PRIDE; Q7TNR6; -.
 ProteomicsDB; 269544; -.
 Antibodypedia; 29423; 80 antibodies from 19 providers.
 DNASU; 230868; -.
 Ensembl; ENSMUST00000039331; ENSMUSP00000046558; ENSMUSG00000040972.
 GeneID; 230868; -.
 KEGG; mmu:230868; -.
 UCSC; uc008vmu.2; mouse.
 CTD; 84966; -.
 MGI; MGI:2681842; Igsf21.
 VEuPathDB; HostDB:ENSMUSG00000040972; -.
 eggNOG; ENOG502QQMY; Eukaryota.
 GeneTree; ENSGT00390000002421; -.
 HOGENOM; CLU_054054_0_0_1; -.
 InParanoid; Q7TNR6; -.
 OMA; RPYTEHP; -.
 OrthoDB; 422073at2759; -.
 PhylomeDB; Q7TNR6; -.
 TreeFam; TF331223; -.
 BioGRID-ORCS; 230868; 3 hits in 71 CRISPR screens.
 ChiTaRS; Igsf21; mouse.
 PRO; PR:Q7TNR6; -.
 Proteomes; UP000000589; Chromosome 4.
 RNAct; Q7TNR6; protein.
 Bgee; ENSMUSG00000040972; Expressed in brain and 85 other tissues.
 Genevisible; Q7TNR6; MM.
 GO; GO:0005912; C:adherens junction; IBA:GO_Central.
 GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
 GO; GO:0060077; C:inhibitory synapse; IDA:UniProtKB.
 GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
 GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
 GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
 GO; GO:0060074; P:synapse maturation; IMP:UniProtKB.
 Gene3D; 2.60.40.10; -; 3.
 InterPro; IPR007110; Ig-like_dom.
 InterPro; IPR036179; Ig-like_dom_sf.
 InterPro; IPR013783; Ig-like_fold.
 InterPro; IPR003599; Ig_sub.
 InterPro; IPR013106; Ig_V-set.
 Pfam; PF07686; V-set; 1.
 SMART; SM00409; IG; 2.
 SUPFAM; SSF48726; SSF48726; 3.
 PROSITE; PS50835; IG_LIKE; 2.
 1: Evidence at protein level;
 Cell junction; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
 Immunoglobulin domain; Lipoprotein; Membrane; Postsynaptic cell membrane;
 Reference proteome; Repeat; Signal; Synapse.
 SIGNAL          1..24
                 /evidence="ECO:0000255"
 CHAIN           25..468
                 /note="Immunoglobulin superfamily member 21"
                 /id="PRO_0000223339"
 DOMAIN          25..132
                 /note="Ig-like 1"
 DOMAIN          344..429
                 /note="Ig-like 2"
 CARBOHYD        82
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        165
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        407
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 DISULFID        46..116
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 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

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