ID G3TT11_LOXAF Unreviewed; 970 AA.
AC G3TT11;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Seizure related 6 homolog like {ECO:0000313|Ensembl:ENSLAFP00000018719.1};
GN Name=SEZ6L {ECO:0000313|Ensembl:ENSLAFP00000018719.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000018719.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000018719.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018719.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000018719.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018719.1};
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; G3TT11; -.
DR Ensembl; ENSLAFT00000035411.1; ENSLAFP00000018719.1; ENSLAFG00000015652.3.
DR GeneTree; ENSGT00940000158873; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; 3.
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:UP000007646};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 903..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..334
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 336..395
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 399..509
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 512..573
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 575..686
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 690..749
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 751..814
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 818..879
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 226..253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 399..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 720..747
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 970 AA; 106358 MW; 762909B03147CA55 CRC64;
SSSSDAHPEG DAGPSGTYPL PWRALESSSL NKDSPEERVT RAPPNPAQSG DQLLELELAG
MAPPTSPDTQ ALSTLLPEQV GTKHTLIPRR KPPSLKQVNT ARKQLRPKAT PTAALQKMHQ
PSSEVPLWLD QKEGTVPTTP APLQISPFTS QPYVAHTLPQ KPDPGEPLGP EESHEASLEE
ASPMTLMDKG GESELTGSAS EENQETTTST IITTTVITTE QAPALCSVSF SDPEGYIDSS
DYPPLPLNNF LECMYNVTVY TGYGVELQVK SVNLSEGELL SIRGVDGPTL TVLANQTLLV
EGQVIRSPTN TISIYFRTFQ EDGLSTFQLH YQAFMLSCSF PHRPDFGDVT VMDLHSGGVA
HFHCHLGYEL QGAKTLTCIN ASKPHWSSPE PICSDPAPCG GAVHNATIGR VLSPSYPGST
NGSQVCVWTI EAPEGQKLHL HFERLSLNEK DRMMVYSGRT NKSALLYDSF QTESVPFEGL
LSDSNTISIE FMSDQARVAS AFNIRFEAFE KGHCYEPYIQ NGNFTTSDAT YNIGTIVEFT
CDPGHSLEQG PAVIECINVR DPYWNDTEPL CRAMCGGELS AVAGVVLSPN WPEPYVEGED
CVWKIHVGEE KRIFLDIQLL NLSNSDILTI YDGDEVMPHI LGQYLGNSGP QKLYSSTPDL
TIQFHSDPAG LIFGKGQGFI MNYIEVSRND SCSDLPEIQN GWKTTSHTEL VRGARITYQC
DPGYDIVGSD TLTCQWDLSW SSDPPFCEKI MYCTDPGEVD HSTRLISDPV LLVGTTIQYT
CNPGFVLEGS SLLTCYSRET GTPIWTSRLP HCVSEESLAC DNPGLPENGY QILYKRLYLP
GESLTFMCYE GFELMGEVTI RCILGQPSHW NGPLPVCKVN QDSFEHALEA EAAAETSLEG
GNMALAIFIP VLIISLVLGG AYIYITRCRY YSNLRLPLMY SHPYSQITVE TEFDNPIYET
GESTAPSVST
//
