ID T2MA21_HYDVU Unreviewed; 663 AA.
AC T2MA21;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Multiple epidermal growth factor-like domains protein 8 {ECO:0000313|EMBL:CDG69118.1};
DE Flags: Fragment;
GN Name=MEGF8 {ECO:0000313|EMBL:CDG69118.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG69118.1};
RN [1] {ECO:0000313|EMBL:CDG69118.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG69118.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
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:PRU00076}.
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DR EMBL; HAAD01002886; CDG69118.1; -; mRNA.
DR AlphaFoldDB; T2MA21; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00055; EGF_Lam; 2.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF01437; PSI; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00180; EGF_Lam; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 99..140
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 174..220
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 221..275
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 273..414
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 444..479
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 192..201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 204..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 243..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 469..478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDG69118.1"
SQ SEQUENCE 663 AA; 74478 MW; 80D616A36933D209 CRC64;
VKHCIWCSEK KKCLYNFQVA MQNKYGECRT VYDGYMLQNC STITNCSSCL NAFHCGWCYD
FIDPRVGRCT IGDFSGPIKK CQIVTIKSEP AWSYEVCPDI NECALNIFSC DINAYCVNTM
YSYECKCKQG YIGDGKSKCI KTCWPECYQG VCNETTYKCE CNLGWTGQNC SVDCGCNGHS
TCLYGVGICD QCQENTVGKY CEKCINGSYG NALTSTGCKK CECNGHGNPL QNYCHSANGE
CFCLHNTIGS SCELCEPGFV GNPRNNGICY IPCKRSSIIS NLYSGYLSPT NEANNLKYTT
CVWLISPRNL TLNEYIYSDP LQFSERILIS ITKINLTSCF DSQLFVYDGI PPNPRSKKVF
IKTSFKKLGR LCGVNSKKVF RSSSGMLSLV YEGQTSKLLL KQDNSNFLIM FQILQCPDHC
PPPYICSVLG ICSCKDGFYG NKCEYSKCIN NCNAKKNQGT CIMDTYCLCK VGFAGEDCSQ
LVSNLFWQIS TMPIHSSAIE NVEDKRFAGT MVIDDSFLYI FGGRNFSDLK SPDVFRVNLL
TGYKEMLNLS SEVCPSSRYF HCSFFYKRNF SKKKVAGHTC TLFGDVVYII GGYYWIDGYS
ICVRLIELNT LKEQYQKFTG PTPSGVPTAE FVSIKVPARG LFAQHNMNDQ DKFKLSQRIA
LLY
//
