SEZ6_BOVIN
ID SEZ6_BOVIN Reviewed; 983 AA.
AC A0JNA2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Seizure protein 6 homolog;
DE Short=SEZ-6;
DE Flags: Precursor;
GN Name=SEZ6;
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=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in cell-cell recognition and in neuronal
CC membrane signaling. Seems to be important for the achievement of the
CC necessary balance between dendrite elongation and branching during the
CC elaboration of a complex dendritic arbor. Involved in the development
CC of appropriate excitatory synaptic connectivity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=Localized on dendrites and in the
CC synaptic and postsynaptic fraction. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEZ6 family. {ECO:0000305}.
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DR EMBL; BC126583; AAI26584.1; -; mRNA.
DR RefSeq; NP_001071486.1; NM_001078018.2.
DR AlphaFoldDB; A0JNA2; -.
DR SMR; A0JNA2; -.
DR STRING; 9913.ENSBTAP00000021257; -.
DR PaxDb; A0JNA2; -.
DR PRIDE; A0JNA2; -.
DR GeneID; 539038; -.
DR KEGG; bta:539038; -.
DR CTD; 124925; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; A0JNA2; -.
DR OrthoDB; 126806at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0050773; P:regulation of dendrite development; IBA:GO_Central.
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; -; 2.
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; 2.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00042; CUB; 2.
DR SUPFAM; SSF49854; SSF49854; 3.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50923; SUSHI; 5.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..983
FT /note="Seizure protein 6 homolog"
FT /id="PRO_0000341347"
FT TRANSMEM 915..935
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 344..403
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 405..516
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 519..580
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 582..693
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 697..756
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 758..821
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 825..886
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 80..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 346..386
FT /evidence="ECO:0000250"
FT DISULFID 372..401
FT /evidence="ECO:0000250"
FT DISULFID 405..432
FT /evidence="ECO:0000250"
FT DISULFID 521..563
FT /evidence="ECO:0000250"
FT DISULFID 548..578
FT /evidence="ECO:0000250"
FT DISULFID 582..608
FT /evidence="ECO:0000250"
FT DISULFID 699..741
FT /evidence="ECO:0000250"
FT DISULFID 727..754
FT /evidence="ECO:0000250"
FT DISULFID 760..802
FT /evidence="ECO:0000250"
FT DISULFID 788..819
FT /evidence="ECO:0000250"
FT DISULFID 827..869
FT /evidence="ECO:0000250"
FT DISULFID 855..884
FT /evidence="ECO:0000250"
SQ SEQUENCE 983 AA; 105923 MW; E1E54A1EE464D0F0 CRC64;
MRPAALLLLP SLLALLVHGL SLEAPTEGEG QAPGLEEMDG ELTAAPTPEQ PEPGVHFVTT
APTLKLLNHH PLLEEFLQEG QEKDELRPDP PTASPLPRLA NQDSRPVFTS PTPVMVAAPT
QPQSREGPWS LESEPPALRI TVALPPGPGM AVPTPGPGER PNTPPPSGAW TPTPEGPGDI
GRPWAPGVMS QTTGLGMEGT VATSTASGDD EETTSTSTII TTAVTTVQPP GPCSWNFSGP
EGSLDSPTAS NSPPDVGLDC FYYISVYPGY GVEIKVQNIS LREGETVTVE GLGGPDPLPL
ANQSFLLRGQ VIRSPTHQAA LRFQSLPPPA GPGTFHFHYQ AYLLSCHFPR RPAYGAVTVT
SLHPGGSARF RCATGYQLKG ARLLTCLNAT QPFWDSQEPV CIAACGGVIR NATTGRIVSP
GFPGNYSNNL TCHWLLEAPE GQRLHLHFEK VSLAEDDDRL IIRNGDNVEA PPVYDSYEVE
YLPIEGLLSS SRHFFVELST DSSGVAAGMA LRYEAFQQGH CYEPFVKYGN FSSSAPSYPV
GTTVEFSCDP GYTLEQGSII IECVDPHDPQ WNETEPACRA VCSGETTDSA GVVLSPNWPE
PYGRGQDCIW GVHVEEDKRI MLDVRVLRIG TGDVLTFYDG DDLTARVLGQ YSGPRGHFKL
FTSMADVTIQ FQSDPGASVL GYQQGFVIHF FEVPRNDTCP ELPEIPNGWK SPSQPELVHG
TVVTYQCYPG YQVVGSSVLM CQWDLTWSED LPSCQRVTSC LDPGDVEHSR RLISSPKFPV
GATVQYICDQ GFVLTGSALL TCHDRQASSP KWSDRTPKCL LEQLKPCHGL SAPENGARSP
EKRLHPAGAT VHFSCAPGYV LKGQASIKCV PGHPSHWSDP PPICRAASLD GFYSGRSLDV
AKVPAASSTL DAAHLAAAIF LPLVAMALLV GGVYLYFCRL QGNSPLQLPR TRPRPYDRIT
VESAFDNPTY ETGSLSFAGD ERI
