IGS21_HUMAN
ID IGS21_HUMAN Reviewed; 467 AA.
AC Q96ID5; Q8NBR8;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Immunoglobulin superfamily member 21 {ECO:0000305};
DE Short=IgSF21 {ECO:0000305};
DE Flags: Precursor;
GN Name=IGSF21 {ECO:0000312|HGNC:HGNC:28246};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP VARIANT [LARGE SCALE ANALYSIS] MET-467.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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:0000250|UniProtKB:Q7TNR6}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q7TNR6}.
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; AK075316; BAC11542.1; -; mRNA.
DR EMBL; AL356101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007618; AAH07618.1; -; mRNA.
DR CCDS; CCDS184.1; -.
DR RefSeq; NP_116269.3; NM_032880.4.
DR AlphaFoldDB; Q96ID5; -.
DR BioGRID; 124396; 42.
DR IntAct; Q96ID5; 31.
DR MINT; Q96ID5; -.
DR STRING; 9606.ENSP00000251296; -.
DR GlyGen; Q96ID5; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96ID5; -.
DR PhosphoSitePlus; Q96ID5; -.
DR BioMuta; IGSF21; -.
DR DMDM; 74760871; -.
DR EPD; Q96ID5; -.
DR jPOST; Q96ID5; -.
DR MassIVE; Q96ID5; -.
DR MaxQB; Q96ID5; -.
DR PaxDb; Q96ID5; -.
DR PeptideAtlas; Q96ID5; -.
DR PRIDE; Q96ID5; -.
DR ProteomicsDB; 76824; -.
DR Antibodypedia; 29423; 82 antibodies from 19 providers.
DR DNASU; 84966; -.
DR Ensembl; ENST00000251296.4; ENSP00000251296.1; ENSG00000117154.12.
DR GeneID; 84966; -.
DR KEGG; hsa:84966; -.
DR MANE-Select; ENST00000251296.4; ENSP00000251296.1; NM_032880.5; NP_116269.3.
DR UCSC; uc001bau.3; human.
DR CTD; 84966; -.
DR DisGeNET; 84966; -.
DR GeneCards; IGSF21; -.
DR HGNC; HGNC:28246; IGSF21.
DR HPA; ENSG00000117154; Tissue enhanced (brain).
DR neXtProt; NX_Q96ID5; -.
DR OpenTargets; ENSG00000117154; -.
DR PharmGKB; PA142671661; -.
DR VEuPathDB; HostDB:ENSG00000117154; -.
DR eggNOG; ENOG502QQMY; Eukaryota.
DR GeneTree; ENSGT00390000002421; -.
DR HOGENOM; CLU_054054_0_0_1; -.
DR InParanoid; Q96ID5; -.
DR OMA; RPYTEHP; -.
DR OrthoDB; 422073at2759; -.
DR PhylomeDB; Q96ID5; -.
DR TreeFam; TF331223; -.
DR PathwayCommons; Q96ID5; -.
DR SignaLink; Q96ID5; -.
DR BioGRID-ORCS; 84966; 6 hits in 1061 CRISPR screens.
DR ChiTaRS; IGSF21; human.
DR GenomeRNAi; 84966; -.
DR Pharos; Q96ID5; Tdark.
DR PRO; PR:Q96ID5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96ID5; protein.
DR Bgee; ENSG00000117154; Expressed in right hemisphere of cerebellum and 116 other tissues.
DR Genevisible; Q96ID5; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0060077; C:inhibitory synapse; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; ISS: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; 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..467
FT /note="Immunoglobulin superfamily member 21"
FT /id="PRO_0000223338"
FT DOMAIN 25..132
FT /note="Ig-like 1"
FT DOMAIN 344..429
FT /note="Ig-like 2"
FT REGION 229..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 245
FT /note="R -> H (in dbSNP:rs2355877)"
FT /id="VAR_056049"
FT VARIANT 379
FT /note="T -> M (in dbSNP:rs12076815)"
FT /id="VAR_056050"
FT VARIANT 467
FT /note="T -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs766575681)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035518"
FT CONFLICT 369
FT /note="E -> G (in Ref. 1; BAC11542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 51835 MW; F62DD2C086A3EDAC CRC64;
MRTAPSLRRC VCLLLAAILD LARGYLTVNI EPLPPVVAGD AVTLKCNFKT DGRMREIVWY
RVTDGGTIKQ KIFTFDAMFS TNYSHMENYR KREDLVYQST VRLPEVRISD NGPYECHVGI
YDRATREKVV LASGNIFLNV MAPPTSIEVV AADTPAPFSR YQAQNFTLVC IVSGGKPAPM
VYFKRDGEPI DAVPLSEPPA ASSGPLQDSR PFRSLLHRDL DDTKMQKSLS LLDAENRGGR
PYTERPSRGL TPDPNILLQP TTENIPETVV SREFPRWVHS AEPTYFLRHS RTPSSDGTVE
VRALLTWTLN PQIDNEALFS CEVKHPALSM PMQAEVTLVA PKGPKIVMTP SRARVGDTVR
ILVHGFQNEV FPEPMFTWTR VGSRLLDGSA EFDGKELVLE RVPAELNGSM YRCTAQNPLG
STDTHTRLIV FENPNIPRGT EDSNGSIGPT GARLTLVLAL TVILELT
