SE6L2_MOUSE
ID SE6L2_MOUSE Reviewed; 910 AA.
AC Q4V9Z5; Q6AXF9; Q91X64;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Seizure 6-like protein 2;
DE AltName: Full=Brain-specific receptor-like protein A;
DE Short=BSRP-A;
DE Flags: Precursor;
GN Name=Sez6l2;
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 [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=16814779; DOI=10.1016/j.febslet.2006.06.043;
RA Miyazaki T., Hashimoto K., Uda A., Sakagami H., Nakamura Y., Saito S.Y.,
RA Nishi M., Kume H., Tohgo A., Kaneko I., Kondo H., Fukunaga K., Kano M.,
RA Watanabe M., Takeshima H.;
RT "Disturbance of cerebellar synaptic maturation in mutant mice lacking
RT BSRPs, a novel brain-specific receptor-like protein family.";
RL FEBS Lett. 580:4057-4064(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Eye, and Salivary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May contribute to specialized endoplasmic reticulum functions
CC in neurons. {ECO:0000269|PubMed:16814779}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16814779}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16814779}. Note=In cerebellar predominantly
CC localized to the endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Named isoforms=3.;
CC Name=1;
CC IsoId=Q4V9Z5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4V9Z5-2; Sequence=VSP_033599;
CC Name=3;
CC IsoId=Q4V9Z5-3; Sequence=VSP_033598, VSP_033599;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the brain, predominantly
CC in the neurons. Wide expression in the gray matter of the brain with
CC high levels in the olfactory bulb, anterior olfactory nuclei,
CC hippocampal formation and cerebellar cortex. Detected diffusely and
CC weakly in the white matter, such as the corpus callosum and cerebellar
CC medulla. In the cerebellar cortex, intensely expressed in Purkinje
CC cells (PC) and granule cells. Detected also in interneurons in the
CC molecular layer. Up-regulated at two weeks after birth.
CC {ECO:0000269|PubMed:16814779}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Sez6, Sez6l1, Sez6l2 exhibit motor
CC discordination, and PCs are ofen innervated by multiple climbing fibers
CC with different neuronal origins in the cerebellum.
CC {ECO:0000269|PubMed:16814779}.
CC -!- SIMILARITY: Belongs to the SEZ6 family. {ECO:0000305}.
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DR EMBL; AK034088; BAC28579.1; -; mRNA.
DR EMBL; AB206789; BAE44442.1; -; mRNA.
DR EMBL; BC011475; AAH11475.1; -; mRNA.
DR EMBL; BC079573; AAH79573.1; -; mRNA.
DR EMBL; BC096615; AAH96615.1; -; mRNA.
DR CCDS; CCDS40135.1; -. [Q4V9Z5-2]
DR CCDS; CCDS57585.1; -. [Q4V9Z5-1]
DR CCDS; CCDS57586.1; -. [Q4V9Z5-3]
DR RefSeq; NP_001239495.1; NM_001252566.1. [Q4V9Z5-1]
DR RefSeq; NP_001239496.1; NM_001252567.1. [Q4V9Z5-3]
DR RefSeq; NP_659175.1; NM_144926.5. [Q4V9Z5-2]
DR AlphaFoldDB; Q4V9Z5; -.
DR SMR; Q4V9Z5; -.
DR IntAct; Q4V9Z5; 1.
DR STRING; 10090.ENSMUSP00000101940; -.
DR GlyGen; Q4V9Z5; 5 sites.
DR iPTMnet; Q4V9Z5; -.
DR PhosphoSitePlus; Q4V9Z5; -.
DR MaxQB; Q4V9Z5; -.
DR PaxDb; Q4V9Z5; -.
DR PeptideAtlas; Q4V9Z5; -.
DR PRIDE; Q4V9Z5; -.
DR ProteomicsDB; 255511; -. [Q4V9Z5-1]
DR ProteomicsDB; 256536; -. [Q4V9Z5-2]
DR ProteomicsDB; 256537; -. [Q4V9Z5-3]
DR Antibodypedia; 54161; 88 antibodies from 17 providers.
DR DNASU; 233878; -.
DR Ensembl; ENSMUST00000106332; ENSMUSP00000101939; ENSMUSG00000030683. [Q4V9Z5-3]
DR Ensembl; ENSMUST00000106333; ENSMUSP00000101940; ENSMUSG00000030683. [Q4V9Z5-2]
DR Ensembl; ENSMUST00000106335; ENSMUSP00000101942; ENSMUSG00000030683. [Q4V9Z5-1]
DR GeneID; 233878; -.
DR KEGG; mmu:233878; -.
DR UCSC; uc009jtq.2; mouse. [Q4V9Z5-2]
DR UCSC; uc009jtr.2; mouse. [Q4V9Z5-1]
DR UCSC; uc012ftx.2; mouse. [Q4V9Z5-3]
DR CTD; 26470; -.
DR MGI; MGI:2385295; Sez6l2.
DR VEuPathDB; HostDB:ENSMUSG00000030683; -.
DR eggNOG; ENOG502QS53; Eukaryota.
DR GeneTree; ENSGT00940000160492; -.
DR HOGENOM; CLU_011474_3_0_1; -.
DR InParanoid; Q4V9Z5; -.
DR OMA; VVTYQCE; -.
DR OrthoDB; 126806at2759; -.
DR PhylomeDB; Q4V9Z5; -.
DR TreeFam; TF330037; -.
DR BioGRID-ORCS; 233878; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Sez6l2; mouse.
DR PRO; PR:Q4V9Z5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q4V9Z5; protein.
DR Bgee; ENSMUSG00000030683; Expressed in supraoptic nucleus and 176 other tissues.
DR ExpressionAtlas; Q4V9Z5; baseline and differential.
DR Genevisible; Q4V9Z5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IGI:MGI.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IGI:MGI.
DR GO; GO:0060074; P:synapse maturation; IGI:MGI.
DR CDD; cd00033; CCP; 5.
DR CDD; cd00041; CUB; 3.
DR Gene3D; 2.60.120.290; -; 3.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00042; CUB; 3.
DR SUPFAM; SSF49854; SSF49854; 3.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS01180; CUB; 3.
DR PROSITE; PS50923; SUSHI; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Sushi;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..910
FT /note="Seizure 6-like protein 2"
FT /id="PRO_0000333889"
FT TOPO_DOM 28..844
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..910
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 173..286
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 288..347
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 349..459
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 462..525
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 527..638
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 642..701
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 703..766
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 769..830
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 70..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..202
FT /evidence="ECO:0000250"
FT DISULFID 290..330
FT /evidence="ECO:0000250"
FT DISULFID 316..345
FT /evidence="ECO:0000250"
FT DISULFID 349..376
FT /evidence="ECO:0000250"
FT DISULFID 464..508
FT /evidence="ECO:0000250"
FT DISULFID 491..523
FT /evidence="ECO:0000250"
FT DISULFID 527..553
FT /evidence="ECO:0000250"
FT DISULFID 644..686
FT /evidence="ECO:0000250"
FT DISULFID 672..699
FT /evidence="ECO:0000250"
FT DISULFID 705..747
FT /evidence="ECO:0000250"
FT DISULFID 733..764
FT /evidence="ECO:0000250"
FT DISULFID 771..813
FT /evidence="ECO:0000250"
FT DISULFID 799..828
FT /evidence="ECO:0000250"
FT VAR_SEQ 71..130
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033598"
FT VAR_SEQ 830
FT /note="V -> VAYEELLDNRKLEV (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:16814779"
FT /id="VSP_033599"
SQ SEQUENCE 910 AA; 97504 MW; 5F58777166A6AA1F CRC64;
MGTPKAQHPP PSQLLLLILL SCAWIEGLPL KEDEMMPEPG SETPTVASED LAELLHGALL
RKGPEIGFLP GSDPDPTLAT PPAGQTLAAP SLPRATEPGT GPLTTAVTPK GVRGAGPTAP
ELLTPPPGTT APPPPGPASP VPPLRPEGGE EETTTTIITT TTVTTTVTSP VLCNNNISEG
EGFVESPDLG STASRSVELL DCTYSIHVYP GYGIEIQVQT LNLSQEEELL VLAGGGSPGL
APRLLANSSM LGEGQVLRSP TNRLLLHFQS PRVPRGNGFR IHYQAYLLSC GFPPRPAHGD
VSVTDLHPGG TATFHCDSGY QLQGEETLIC LNGTRPAWTG EPPSCTASCG GTIHNATLGR
IVSPEPGGAA GPNLTCRWVI EAAEGRRLHL HFERVSLDED NDRLMVRSGG SPLSPVIYDS
DMDDVPERGL ISDAQSLYVE LLSETPANPL LLSLRFEAFE EDRCFPPFLA HGNVTTTDPE
FHPGALATFS CLPGYALEPP GPPNAIECVD PTEPHWNDTE PACKAMCGGE LSEPAGVVLS
PDWPQSYSPG QDCVWGLHVQ EEKRILLQVE ILNVREGDML TLFDGDGPSA RVLAQLRGPQ
PRRRLLSSGP DLTLQFQAPP GPPNPGLGQG FVLHFKEVPR NDTCPELPPP EWGWRTASHG
DLIRGTVLTY QCEPGYELLG SDILTCQWDL SWSAAPPACQ KIMTCADPGE ITNGHRTASD
AGFPVGSHVQ YRCLPGYSLE GAAVLTCYSR DTGTPKWSDR VPKCALKYEP CLNPGVPENG
YQTLYKHHYQ AGESLRFFCY EGFELIGEVT ITCVPGHPSQ WTSQPPLCKV TQTTDPSRQL
EGGNLALAIL LPLGLVIVLG IGVYIYYTKL QGKSLFGFSG SHSYSPITVE SDFSNPLYEA
GDTREYEVSI
