IGSF3_MOUSE
ID IGSF3_MOUSE Reviewed; 1194 AA.
AC Q6ZQA6; A0A4X9; Q7TPV3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Immunoglobulin superfamily member 3;
DE Short=IgSF3;
DE Flags: Precursor;
GN Name=Igsf3; Synonyms=Kiaa0466;
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 TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Osteoblast;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 717-1194.
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1077.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=24372406; DOI=10.1111/cge.12321;
RA Foster J., Kapoor S., Diaz-Horta O., Singh A., Abad C., Rastogi A.,
RA Moharana R., Tekeli O., Walz K., Tekin M.;
RT "Identification of an IGSF3 mutation in a family with congenital
RT nasolacrimal duct obstruction.";
RL Clin. Genet. 86:589-591(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the lacrimal duct and lacrimal gland.
CC {ECO:0000269|PubMed:24372406}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the lacrimal duct at embryonic day
CC (E)19 and in both the lacrimal duct and lacrimal gland at post natal
CC day (P)30. {ECO:0000269|PubMed:24372406}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97961.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK129151; BAC97961.1; ALT_INIT; mRNA.
DR EMBL; BC052892; AAH52892.1; -; mRNA.
DR EMBL; AK052454; BAC35000.1; -; mRNA.
DR CCDS; CCDS17682.1; -.
DR RefSeq; NP_997088.2; NM_207205.2.
DR AlphaFoldDB; Q6ZQA6; -.
DR STRING; 10090.ENSMUSP00000048900; -.
DR GlyConnect; 2383; 3 N-Linked glycans (3 sites).
DR GlyGen; Q6ZQA6; 6 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q6ZQA6; -.
DR PhosphoSitePlus; Q6ZQA6; -.
DR MaxQB; Q6ZQA6; -.
DR PaxDb; Q6ZQA6; -.
DR PeptideAtlas; Q6ZQA6; -.
DR PRIDE; Q6ZQA6; -.
DR ProteomicsDB; 267303; -.
DR Antibodypedia; 46948; 183 antibodies from 27 providers.
DR DNASU; 78908; -.
DR Ensembl; ENSMUST00000043983; ENSMUSP00000048900; ENSMUSG00000042035.
DR GeneID; 78908; -.
DR KEGG; mmu:78908; -.
DR UCSC; uc008qrg.2; mouse.
DR CTD; 3321; -.
DR MGI; MGI:1926158; Igsf3.
DR VEuPathDB; HostDB:ENSMUSG00000042035; -.
DR eggNOG; ENOG502QRRB; Eukaryota.
DR GeneTree; ENSGT00940000155177; -.
DR HOGENOM; CLU_005187_0_0_1; -.
DR InParanoid; Q6ZQA6; -.
DR OMA; AYAVYSQ; -.
DR PhylomeDB; Q6ZQA6; -.
DR TreeFam; TF332702; -.
DR BioGRID-ORCS; 78908; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Igsf3; mouse.
DR PRO; PR:Q6ZQA6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6ZQA6; protein.
DR Bgee; ENSMUSG00000042035; Expressed in humerus cartilage element and 199 other tissues.
DR ExpressionAtlas; Q6ZQA6; baseline and differential.
DR Genevisible; Q6ZQA6; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0032808; P:lacrimal gland development; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 8.
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; 4.
DR SMART; SM00409; IG; 8.
DR SMART; SM00406; IGv; 4.
DR SUPFAM; SSF48726; SSF48726; 8.
DR PROSITE; PS50835; IG_LIKE; 8.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1194
FT /note="Immunoglobulin superfamily member 3"
FT /id="PRO_0000320135"
FT TOPO_DOM 20..1124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1125..1145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1146..1194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..138
FT /note="Ig-like C2-type 1"
FT DOMAIN 143..262
FT /note="Ig-like C2-type 2"
FT DOMAIN 276..386
FT /note="Ig-like C2-type 3"
FT DOMAIN 401..539
FT /note="Ig-like C2-type 4"
FT DOMAIN 545..661
FT /note="Ig-like C2-type 5"
FT DOMAIN 676..803
FT /note="Ig-like C2-type 6"
FT DOMAIN 813..945
FT /note="Ig-like C2-type 7"
FT DOMAIN 949..1097
FT /note="Ig-like C2-type 8"
FT REGION 997..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 250..252
FT /note="EWI motif"
FT COMPBIAS 1008..1024
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 42..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 167..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 302..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 432..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 566..645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 701..782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 838..918
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 974..1080
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 523
FT /note="E -> G (in Ref. 2; AAH52892)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="E -> D (in Ref. 2; AAH52892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1194 AA; 134710 MW; 2A76F53A8B1FD3C3 CRC64;
MKCFFPVLSC LAVLGVVSAQ RQVTVQEGPL YRTESSHITI WCNVSGYQGP SEQNFQWSIY
LPSAPEREVQ IVSTVDSSFP YAIYTQRVRG GKIYVERIQG NSALLHITDL QARDAGEYEC
HTPNTDERYF GSYSAKMNLV VIPDSLQTTA VPQTLHKVEQ DPLELSCEVA TETVQHTHLS
VSWLRQKGGE NPVEVISLSR DFILHSSSEY AQRQSLGEVR LDKLGRSTFR LTIFHLQPSD
QGEFYCEAAE WIQDPDGSWY AMTRKRSEGA VVNVQPTDKE FTVRLETDKR LHTVGEPVEF
RCILEAQNIP DRYFAVSWAF NSSLIATMGP NAVPVLNSDF AHREAKGQLK VAKESDGVFV
LKIYHLRQED SGKYNCRVTE REKTVTGEFI DKESKRPKNI PIVVLPLKSS ISVEVASNAS
VVLEGEDLHF SCTVRTVGRL QARFSVIWQL VDRQNRRSNV MWLDRDGTLQ PGSAYWERSS
YGGIQMEQVQ PNSFSLGIFN SRKEDEGQYE CHVTEWVRAV DGEWQIVGER RASTLVSITA
LETGFAVTAI SRTPGVTYSD SFDLQCIIKP HYPARVPVSV TWRFQPVGTV EFHDLVTFTR
DGGVQWGDKS STFRTRTAIE KAESSNNVRL SISRASDTEA GKYQCVAELW RRNYNNTWTR
LAERTSNLLE IRVLQPVTKL QVSKSKRTLT LVENRAIQLN CSVKSQTSPN SHFAVLWYVH
KPSDADGKLI LKTTHSSAFE YGTYAEEEGL RGRLQFERHV SGGLFSLTVQ RAEVSDSGSY
YCHVEEWLLS PNYAWYKLAE EVSGRTEVTV KQPDSRLKLS QVQGSLSVLE TRQIQLECVV
LNRTSVASQL LVEWFVWKPN HPEREVVAHL SRDATFHYGE QAAKNNLKGR LHAESPSSGV
YRLFIQNVAV QDSGTYSCRV EEWLPSPSGV WYKRAEDTAG QTAVTVMRPD AALQVDTVVP
NATVTEKAAF QLDCSILSRS SQDSRFAVAW YSLRTKGGGK RGSLGIDEQE EEEEEEDISQ
EEDSEDPTER TVLLSVGPDA VFGPEGSPWE GRLRFQRLSP LLYRLTVLEA SPQDTGNYSC
HVEEWLPSPQ KEWYRLTEEE SAPIGIRVLD TSSTLQSLIC SNDALFYFVF FYPFPIFGIL
IITILLVRFK SRNSSKNSEG KNGVPLLWIK EPHLNYSPTC LEPPVLSIHP GAID
