SEZ6_XENLA
ID SEZ6_XENLA Reviewed; 900 AA.
AC Q6AX42;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Seizure protein 6 homolog;
DE Short=SEZ-6;
DE Flags: Precursor;
GN Name=sez6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in cell-cell recognition and in neuronal
CC membrane signaling. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEZ6 family. {ECO:0000305}.
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DR EMBL; BC079770; AAH79770.1; -; mRNA.
DR RefSeq; NP_001087427.1; NM_001093958.1.
DR AlphaFoldDB; Q6AX42; -.
DR SMR; Q6AX42; -.
DR DNASU; 447251; -.
DR GeneID; 447251; -.
DR KEGG; xla:447251; -.
DR CTD; 447251; -.
DR Xenbase; XB-GENE-921463; sez6l2.S.
DR OrthoDB; 126806at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 447251; Expressed in brain and 13 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00033; CCP; 5.
DR CDD; cd00041; CUB; 2.
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; 2.
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; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..900
FT /note="Seizure protein 6 homolog"
FT /id="PRO_0000341349"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 151..259
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 261..320
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 322..436
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 439..500
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 502..613
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 617..676
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 678..741
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 744..805
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 111..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..178
FT /evidence="ECO:0000250"
FT DISULFID 263..303
FT /evidence="ECO:0000250"
FT DISULFID 289..318
FT /evidence="ECO:0000250"
FT DISULFID 322..353
FT /evidence="ECO:0000250"
FT DISULFID 441..483
FT /evidence="ECO:0000250"
FT DISULFID 468..498
FT /evidence="ECO:0000250"
FT DISULFID 502..528
FT /evidence="ECO:0000250"
FT DISULFID 619..661
FT /evidence="ECO:0000250"
FT DISULFID 647..674
FT /evidence="ECO:0000250"
FT DISULFID 680..722
FT /evidence="ECO:0000250"
FT DISULFID 708..739
FT /evidence="ECO:0000250"
FT DISULFID 746..788
FT /evidence="ECO:0000250"
FT DISULFID 774..803
FT /evidence="ECO:0000250"
SQ SEQUENCE 900 AA; 98394 MW; B3A399099706BEDD CRC64;
MMPLAGIAWN LMLLFSAVQG LPLQDGEGTQ HPDLLNNPPK GSVEPVALEQ LVHQAILKKD
FLAQDVFFPG TTAIPTRAAP ISLTEGVSDA SGVLTTAVGG AFSLPPQLST LIPPSPAPTG
GPGPSPEAEE ETTTTLITTT TVTTVHSPVL CNNNISESEG LLEAPEYGGS TFFGGLDCTY
SVSVYLGYGV EIRVERLNLS KEEALSIEGL EEDRRFLLAN ETLMAEGQVI RSPTNHVAVR
FQTYRATSPG AFRLRYQAFV LSCVFPPRPE NGEVTVTDLH PGGAANFRCS AGFTLKGGES
LVCLNISRPE WSGKPPVCAA SCGGVIRNAT VGRIVSPDIS TSHSNNHGNN LSCHWLIEAA
EGQRLHLHFE RVSLDEDNDR LVVRSGSSPL SPVIYDSDID DVPERGLLSD AQSLYIELIS
DNPAVPLLLS LRYEVFSESR CYEPFLAHGN FTTTDPLYSP GSLVSFFCNA GYMLEQGPPV
IECVDPADPH WNESEPVCKA LCGGEISEPA GVILSPDWPQ NYGKGQDCVW GIHVQEDRRV
LLEIEILNIR RSDALTVYDG DDLTARVLGQ YMGVHQRFNL FSSANDVTLQ FQSDSNDPVF
SLSQGFIIHF KEVPRNDTCP ALPEVPNGWK TSSHPDLIRG TVVTYQCEPG YDISGSDILT
CQWDLSWSNA PPTCEKILNC ADPGEIANGV RRASDPRFPI GSHVQYSCNE GYTLEGSRTL
TCYNRDTGTP KWSDRIPKCV LKYEPCLNPG VPENGYQTLY KHHYQAGEAL RFFCYEGFEL
IGEVTITCAP GHPSQWTSQP PLCKVAYEEL LDDRKLEVTQ TTDPSHQMEG GNIALAIFLP
IILVILLIGG IYIYYTKFQG KSLFGFSFPA SHSYSPITVE SDFNNPLYEA GDTREYEVSI
