SE6L2_BOVIN
ID SE6L2_BOVIN Reviewed; 910 AA.
AC Q29RN8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Seizure 6-like protein 2;
DE Flags: Precursor;
GN Name=SEZ6L2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May contribute to specialized endoplasmic reticulum functions
CC in neurons. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEZ6 family. {ECO:0000305}.
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DR EMBL; BC114092; AAI14093.1; -; mRNA.
DR RefSeq; NP_001039392.1; NM_001045927.2.
DR AlphaFoldDB; Q29RN8; -.
DR SMR; Q29RN8; -.
DR STRING; 9913.ENSBTAP00000010460; -.
DR PaxDb; Q29RN8; -.
DR PRIDE; Q29RN8; -.
DR Ensembl; ENSBTAT00000010460; ENSBTAP00000010460; ENSBTAG00000007955.
DR GeneID; 505735; -.
DR KEGG; bta:505735; -.
DR CTD; 26470; -.
DR VEuPathDB; HostDB:ENSBTAG00000007955; -.
DR VGNC; VGNC:34504; SEZ6L2.
DR eggNOG; ENOG502QS53; Eukaryota.
DR GeneTree; ENSGT00940000160492; -.
DR HOGENOM; CLU_011474_3_0_1; -.
DR InParanoid; Q29RN8; -.
DR OrthoDB; 126806at2759; -.
DR TreeFam; TF330037; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000007955; Expressed in Ammon's horn and 39 other tissues.
DR ExpressionAtlas; Q29RN8; baseline.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IBA:GO_Central.
DR GO; GO:0060074; P:synapse maturation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..910
FT /note="Seizure 6-like protein 2"
FT /id="PRO_0000333887"
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 92..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..191
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 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
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 355
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 CARBOHYD 641
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"
SQ SEQUENCE 910 AA; 97508 MW; BA40D92FC77382E5 CRC64;
MGTPRAQHPP PPQLLFLFLL SCPWIQGLPL KEEEALPEPG SETPTVASEA LAELLHGALL
RKGPEMGYLP GSDPDPTLAT PPVGQTIAAP FLPRATEPGT GPLTTAVTPK GGRGAGPTAP
ELLTPPPGTT APPLPGPASP GPPLGPEGGE EETTTTIITT TTVTTTVTSP VLCNNNISEG
EGHVESPDLG SSTSRTLGLL DCTYSIHVYP GYGIEIQVQM LNLSREEELL VLAGGGSPGL
APRLLANSSM LGEGQVLRSP TNRLLLHFQS PRVPRGAGFR IHYQAYLLSC GFPPQPAHGD
VSVTDLHPGG TATFHCDSGY QLQGEETLVC LNGTRPAWSS EPPSCMASCG GTIHNATLGR
IVSPEPGGAA GPNLTCRWVI EAAEGRRLHL HFERVSLDED NDRLMVRSGG SPLSPVIYDS
DMDDVPERGL ISDAQSLYVE LLSETPANPL LLSLRFEAFE EDRCFAPFLA HGNVTTTDPE
YRPGALATFS CLPGYALEPP GPPNVIECVD PTEPHWNDTE PACKAMCGGE LSEPAGVVLS
PDWPQSYSPG QDCVWGLHVQ EEKRILLQVE ILNVREGDML TLFDGDGPSA RVLAQLRGPQ
PRRRLLSSGS DLTLQFQAPP GPPNPGLGQG FVLHFKEVPR NDTCPELPPP EWGWRTASHG
DLIRGTVLTY QCEPGYELLG SDILTCQWDL SWSAAPPACQ KIMTCADPGE ITNGHRTTSD
AGFPVGSHVQ YRCLPGYSLE GAAVLTCYSR DTGTPKWSDR VPKCALKYEP CLNPGVPENG
YQTLYKHHYQ AGESLRFFCY EGFELIGEVT ITCVPGHPSQ WTSQPPLCKV TQTTDPSRQL
EGGNLALAIL LPLGLVIILG SGVYIYYTKL QGKSLFGFSG SHSYSPITVE SDFSNPLYEA
GDTREYEVSI
