ID A0A452E273_CAPHI Unreviewed; 1000 AA.
AC A0A452E273;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Seizure related 6 homolog like {ECO:0000313|Ensembl:ENSCHIP00000006111.1};
GN Name=SEZ6L {ECO:0000313|Ensembl:ENSCHIP00000006111.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000006111.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000006111.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000006111.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; LWLT01000018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452E273; -.
DR STRING; 9925.ENSCHIP00000006111; -.
DR Ensembl; ENSCHIT00000013822.1; ENSCHIP00000006111.1; ENSCHIG00000009959.1.
DR GeneTree; ENSGT00940000158873; -.
DR Proteomes; UP000291000; Chromosome 17.
DR Bgee; ENSCHIG00000009959; Expressed in prefrontal cortex and 14 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 5.
DR CDD; cd00041; CUB; 3.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 5.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 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 PANTHER; PTHR45656; PROTEIN CBR-CLEC-78; 1.
DR PANTHER; PTHR45656:SF8; SEIZURE 6-LIKE PROTEIN; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00042; CUB; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 5.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR PROSITE; PS01180; CUB; 3.
DR PROSITE; PS50923; SUSHI; 5.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 933..955
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..365
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 367..426
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 428..538
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 541..602
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 604..715
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 719..778
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 780..843
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 847..908
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 257..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 428..455
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 749..776
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1000 AA; 109051 MW; 1F27F47D15DC507A CRC64;
PFSFHPPQPG LQGLPTPLCS PPEGDAGQSD TYLLPSEILG SSSLSKENPE ESVTTAPLNP
VQSGDELREP ELEGTVPFAP QDPAAVSTLL PHAFPARKKP PSLKQVNLAR KQLRPKATPA
AATQRTASQP ASPGPGLLAA APGKPRPPGD QDPVASEPLW LERKEGAVPT TPAPLQIAPF
TSQPLVAHTL PQSPEPGAPA VPEEAPEAPL EDASPGTLMD KGETELAGSA SEESQETTTS
TIITTTVITT EQAPAVCSVS FSDPEGYIDS SDYPPLPLHN FLECTYNATV YTGYGVELQV
KSVNLSEGEL LSIRGVDGPS LTVLANHTLL VEGQVIRSPT NTISVYFRTF QDDGLGTFQL
HYQAFMLSCS FPRRPDFGDV TVMDLHSGGE AHFHCHLGYE LQGAKTLTCI NASKPHWSSR
EPICSAPCGG AVHNATIGRV LSPSHSANAS GSQFCVWTIE APEGQKLHLH FERLALHEKD
RMMVYSGLTN KSTLLYDSFQ TDNVPFEGLL SDGHTIRIEF TSHQPPAASA FNIRFEAFEK
GHCYEPYIQN GNFTTSDPTY NIGTIVEFTC DPGHSLEQGP AVIECINVRD PYWNDTEPLC
RAMCGGELSA VAGVVLSPNW PEPYVEGEDC IWKIHVGEEK RIFLDIQFLN LSNSDILTIY
DGDEVMPHIL GQYLGNSGPQ KLYSSTPDLT IQFHSDPAGL IFGKGQGFIM NYIEVSRNDS
CSDLPEIQNG WKTTSHTELV RGARITYQCD PGYDIVGSDT LTCQWDLSWS SDPPFCEKIM
YCTDPGEVDH STRLISDPVL LVGTTIQYTC NPGFVLEGSS LLTCYSRETG SPIWTSRLPH
CVSEESLACD NPGLPENGYQ ILYKRLYLPG ESLTFMCYEG FELMGEVTIR CILGQPSHWS
GPLPVCKVNQ DSFEHALEVA EAAAETSLEG GNMALAIFIP VLIISLLLGG AYIYITRCRY
YSNLRLPLMY SHPYSQITVE TEFDNPIYET GETREYEVSI
//
