SE6L1_MOUSE
ID SE6L1_MOUSE Reviewed; 963 AA.
AC Q6P1D5; Q3V651; Q499M3; Q6PHN6; Q8C420;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Seizure 6-like protein;
DE AltName: Full=Acupuncture-induced protein 1-L;
DE AltName: Full=Brain-specific receptor-like protein B;
DE Short=BSRP-B;
DE Flags: Precursor;
GN Name=Sez6l; Synonyms=Aig1l, Kiaa0927;
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; TISSUE=Brain;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=17341691; DOI=10.1152/physiolgenomics.00057.2006;
RA Takaoka Y., Ohta M., Ito A., Takamatsu K., Sugano A., Funakoshi K.,
RA Takaoka N., Sato N., Yokozaki H., Arizono N., Goto S., Maeda E.;
RT "Electroacupuncture suppresses myostatin gene expression: cell
RT proliferative reaction in mouse skeletal muscle.";
RL Physiol. Genomics 30:102-110(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Candidate tumor suppressor gene. May contribute to
CC specialized endoplasmic reticulum functions in neurons. {ECO:0000250,
CC ECO:0000269|PubMed:16814779}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16814779};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:16814779}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:16814779}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16814779}. Note=In
CC cerebellar predominantly localized to the endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1D5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1D5-2; Sequence=VSP_033594;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the brain, predominantly
CC in neurons. Wide expression in the gray matter of the brain with high
CC levels in the olfactory bulb, anterior olfactory nuclei, hippocampal
CC formation and cerebellar cortex. Detected diffusely and weakly in the
CC white matter, such as the corpus callosum and cerebellar medulla. In
CC the cerebellar cortex, intensely expressed in Purkinje cells and
CC granule cells. Detected also in interneurons in the molecular layer.
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; AB206790; BAE44443.1; -; mRNA.
DR EMBL; DQ167195; AAZ99451.1; -; mRNA.
DR EMBL; AK083229; BAC38818.1; -; mRNA.
DR EMBL; BC056471; AAH56471.1; -; mRNA.
DR EMBL; BC065117; AAH65117.1; -; mRNA.
DR EMBL; BC065129; AAH65129.1; -; mRNA.
DR EMBL; BC099839; AAH99839.1; -; mRNA.
DR CCDS; CCDS57373.1; -. [Q6P1D5-1]
DR RefSeq; NP_001240845.1; NM_001253916.1. [Q6P1D5-1]
DR RefSeq; NP_001240846.1; NM_001253917.1.
DR RefSeq; NP_064366.2; NM_019982.3.
DR RefSeq; XP_006535221.1; XM_006535158.3. [Q6P1D5-2]
DR AlphaFoldDB; Q6P1D5; -.
DR SMR; Q6P1D5; -.
DR STRING; 10090.ENSMUSP00000078454; -.
DR GlyConnect; 2692; 2 N-Linked glycans (1 site).
DR GlyGen; Q6P1D5; 11 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q6P1D5; -.
DR PhosphoSitePlus; Q6P1D5; -.
DR MaxQB; Q6P1D5; -.
DR PaxDb; Q6P1D5; -.
DR PRIDE; Q6P1D5; -.
DR ProteomicsDB; 255509; -. [Q6P1D5-1]
DR ProteomicsDB; 255510; -. [Q6P1D5-2]
DR Antibodypedia; 54796; 68 antibodies from 17 providers.
DR Ensembl; ENSMUST00000079491; ENSMUSP00000078454; ENSMUSG00000058153. [Q6P1D5-1]
DR GeneID; 56747; -.
DR KEGG; mmu:56747; -.
DR UCSC; uc008yti.2; mouse. [Q6P1D5-1]
DR UCSC; uc012ebi.2; mouse. [Q6P1D5-2]
DR CTD; 23544; -.
DR MGI; MGI:1935121; Sez6l.
DR VEuPathDB; HostDB:ENSMUSG00000058153; -.
DR eggNOG; ENOG502QVYR; Eukaryota.
DR GeneTree; ENSGT00940000158873; -.
DR InParanoid; Q6P1D5; -.
DR PhylomeDB; Q6P1D5; -.
DR TreeFam; TF330037; -.
DR BioGRID-ORCS; 56747; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Sez6l; mouse.
DR PRO; PR:Q6P1D5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P1D5; protein.
DR Bgee; ENSMUSG00000058153; Expressed in cortical plate and 114 other tissues.
DR ExpressionAtlas; Q6P1D5; baseline and differential.
DR Genevisible; Q6P1D5; 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; 3.
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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..963
FT /note="Seizure 6-like protein"
FT /id="PRO_0000333886"
FT TOPO_DOM 32..897
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..963
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 221..329
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 331..390
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 392..502
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 505..566
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 568..679
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 683..742
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 744..807
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 811..872
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 28..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 221..248
FT /evidence="ECO:0000250"
FT DISULFID 333..373
FT /evidence="ECO:0000250"
FT DISULFID 359..388
FT /evidence="ECO:0000250"
FT DISULFID 392..419
FT /evidence="ECO:0000250"
FT DISULFID 507..549
FT /evidence="ECO:0000250"
FT DISULFID 534..564
FT /evidence="ECO:0000250"
FT DISULFID 568..594
FT /evidence="ECO:0000250"
FT DISULFID 685..727
FT /evidence="ECO:0000250"
FT DISULFID 713..740
FT /evidence="ECO:0000250"
FT DISULFID 746..788
FT /evidence="ECO:0000250"
FT DISULFID 774..805
FT /evidence="ECO:0000250"
FT DISULFID 813..855
FT /evidence="ECO:0000250"
FT DISULFID 841..870
FT /evidence="ECO:0000250"
FT VAR_SEQ 807..872
FT /note="SEESLACDNPGLPENGYQILYKRLYLPGESLTFMCYEGFELMGEVTIRCILG
FT QPSHWSGPLPICKV -> F (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16814779"
FT /id="VSP_033594"
FT CONFLICT 883
FT /note="A -> VA (in Ref. 4; AAH56471/AAH99839)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="Missing (in Ref. 1; BAE44443, 2; AAZ99451, 3;
FT BAC38818 and 4; AAH65117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 963 AA; 104827 MW; 722D6CA2F97B171F CRC64;
MPVARPQAAG PDRISLFLVA FLLGSPAAAQ AEDGGPEGEM HPSTAYLLPS ASLESSLEEG
VTSAAPGLLP SQEALEAMEE SLPPALPDEA SVQHTPALRK GLPSLKQLNS ARRQLRPLAT
PTTLQRLGSP ASATTKLREP EDPEQPTAPA PLQIAPFTAL ATTLPHSPQP AQAPDDSSPG
SPLDKGDNEL TGSASEESQE TTTSTIVTTT IITTEQAPAL CGVSFSDPEG YIDSSDFPPQ
PYSSFLECTY NVTVYTGYGV ELQVKSVNLS EGELLSIRGV DGPTLTVLAN QTLLVEGQVI
RSPTNTISVY FRTFQDDGLG TFQLHYQAFM LSCPFPRRPD AGEVTVMDLH SGGVAHFHCH
LGYELQGAKT LTCINASKPH WSSQEPVCSA PCGGAVHNAT IGRVLSPSFP GTANGSQLCV
WTIEAPEGQK LHLHLERLLL HEKDRMIVYS GRTNTSALLY DSLRTESVPF EGLLSEGSSI
RIEFTSDQGQ AASAFNIRFE AFEKGHCYEP YIQNGNFTTS DPTYNIGTIV EFTCDPGHSL
EQGPAVIECV NVRDPYWNDT EPLCRAMCGG ELSAVAGVVL SPNWPEPYAE GEDCVWKIHV
GEEKRIFLDI QFLNLSNSDI LTIYDGDEVV PHVLGQYFGH SSPQKLYSST PDLTIQFHSD
PAGLIFGKGQ GFIMNYIEVS RNDSCSDLPE IQNGWKTTSH TELVRGARIT YQCDPGYDIV
GSDTLTCQWD LSWSSDPPFC EKIMYCTDPG EVEHSTRLIS DPVLLVGTTI QYTCSPGFVL
EGSSLLTCYS RETGTPIWTS RLPHCVSEES LACDNPGLPE NGYQILYKRL YLPGESLTFM
CYEGFELMGE VTIRCILGQP SHWSGPLPIC KVNQDSFEHA LEAEAAAESS LEGGNMALAI
FIPVLLISLL LGGAYIYVTR CRQYSSLRLP LMYSHPYSQI TVETEFDNPI YETGETREYE
VSI
