IGS21_RAT
ID IGS21_RAT Reviewed; 468 AA.
AC M0RAS4;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 3.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Immunoglobulin superfamily member 21 {ECO:0000305};
DE Short=IgSF21 {ECO:0000305};
DE Flags: Precursor;
GN Name=Igsf21 {ECO:0000312|RGD:1310117};
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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:0000250|UniProtKB:Q7TNR6}.
CC -!- SUBUNIT: Interacts (Ig-like 1 domain) with NRXN2 (via Laminin G-like 1
CC domain) in a trans-interaction manner. {ECO:0000250|UniProtKB:Q7TNR6}.
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. {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:0000250|UniProtKB:Q7TNR6}.
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DR EMBL; AABR07050255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07050256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07050257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07050258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07050259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001258383.1; NM_001271454.1.
DR RefSeq; XP_017448798.1; XM_017593309.1.
DR AlphaFoldDB; M0RAS4; -.
DR STRING; 10116.ENSRNOP00000066631; -.
DR PaxDb; M0RAS4; -.
DR PRIDE; M0RAS4; -.
DR Ensembl; ENSRNOT00000074336; ENSRNOP00000066631; ENSRNOG00000049959.
DR GeneID; 298591; -.
DR KEGG; rno:298591; -.
DR CTD; 84966; -.
DR RGD; 1310117; Igsf21.
DR eggNOG; ENOG502QQMY; Eukaryota.
DR GeneTree; ENSGT00390000002421; -.
DR HOGENOM; CLU_054054_0_0_1; -.
DR InParanoid; M0RAS4; -.
DR OrthoDB; 422073at2759; -.
DR PRO; PR:M0RAS4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060077; C:inhibitory synapse; ISS:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; 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; ISS: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 2: Evidence at transcript 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_0000444205"
FT DOMAIN 25..132
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 344..429
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 46..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 468 AA; 52044 MW; A1C760624CB0B631 CRC64;
MRAAPSLRRA SCLLLAAILD LARGYLTVNI EPLPPVVAGD AVTLKCNFKT DGRMREIVWY
RVTDGGTIKQ KIFTFDAMFS TNYSHMENYR KREDLVYQST VRLPEVRISD NGPYECHVGI
YDRATREKVV LASGNIFLNV MAPPTSIEVV AADSPAPFSR YQAQNFTLVC IVSGGKPAPM
VYFKRDGEPI DAVPLTELPA SSSGSVQDSR PFRSLLHRDV DDTKMQKSLS LLDTEYRAGR
PYTERPSRSL TQDPNLFVQP TTENIPETVV SREFPRWVHS AEPVYFLRHS RTPGSDGTVE
VRALLTWTLN PQIDNEALFS CEVKHPALSM PMQAEVTLVA PKGPKIMMTP SRARVGDTVR
ILVHGFQNEV FPEPMFTWTR VGSRLLDGSA EFDGKELVLE RVPAELNGSM YRCTAQNPLG
STDTHTRLIV FENPNIPRGT EDSRGSASGP TGVRLTLVLA LTVILELT
