ID W5MT17_LEPOC Unreviewed; 565 AA.
AC W5MT17;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Discoidin, CUB and LCCL domain containing 2 {ECO:0000313|Ensembl:ENSLOCP00000011526.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011526.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011526.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; AHAT01003485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MT17; -.
DR STRING; 7918.ENSLOCP00000011526; -.
DR Ensembl; ENSLOCT00000011543.1; ENSLOCP00000011526.1; ENSLOCG00000009438.1.
DR eggNOG; ENOG502QRMB; Eukaryota.
DR GeneTree; ENSGT00940000158147; -.
DR HOGENOM; CLU_016654_2_0_1; -.
DR InParanoid; W5MT17; -.
DR OMA; TKHPPHL; -.
DR Proteomes; UP000018468; Linkage group LG17.
DR Bgee; ENSLOCG00000009438; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.170.130.20; LCCL-like domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR004043; LCCL.
DR InterPro; IPR036609; LCCL_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806:SF3; DISCOIDIN, CUB AND LCCL DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF03815; LCCL; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00603; LCCL; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF69848; LCCL domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50820; LCCL; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00059};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 467..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..153
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 155..251
FT /note="LCCL"
FT /evidence="ECO:0000259|PROSITE:PS50820"
FT DOMAIN 258..415
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 419..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 38..65
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 565 AA; 62932 MW; B19005CAF3D1897B CRC64;
MATVGMVRAE TNGAGIFFIS TFIILSTRTS RAQKGDGCGY TVLGPNSGTL SSIKYPHTYP
NHTVCEWEIH VSQGKKVHFK FGDFDIEDSD SCHFNYLRIY NGIGPTRTEI GKYCGLGMQW
DQLIESTGNE VTVQFMSGMH RSGRGFFLSY STTDHPDLIT CLDKGIHFFD PEFSKYCPAG
CQTPFGEISG NIPHGYRDSS LICMAGIHAG VVSNVLGGQI SVVSSKGIPY YESALANNIT
SVVGPLSNSL FTFKTSGCYG TLGLESRVVH NSQISASSVW EWEDVNGQPS VWGPEGARLK
KPGVPWAVTV NNQNQWLQVD LKKEKRITGI TTTGSTLKDY YYYVSSYRVL YSHDGQQWTV
FRETNTDQDK IFQGNTNYLQ EVRNNFIPPI EARFIRINPT QWHQRIAMKF ELLGCQPHTG
SPKVRAPPPR PPPKISTDFP PLYDKTTYTP DIKNTTMAPS GNKDVTLAAV LVPVLVMALT
VLILFLVCAW HWKNRKKSAE GAYDLPHWDR AGWWKGMKQF LPTKGSEVEE SPVRYSSSEV
SRLRAREGAP VLQAEPAGMK HLHGL
//
