ID T2M797_HYDVU Unreviewed; 436 AA.
AC T2M797;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE SubName: Full=Sphingomyelin synthase-related protein 1 {ECO:0000313|EMBL:CDG67984.1};
GN Name=SAMD8 {ECO:0000313|EMBL:CDG67984.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG67984.1};
RN [1] {ECO:0000313|EMBL:CDG67984.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG67984.1};
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:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000256|ARBA:ARBA00005441}.
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DR EMBL; HAAD01001752; CDG67984.1; -; mRNA.
DR AlphaFoldDB; T2M797; -.
DR EnsemblMetazoa; XM_012704376.1; XP_012559830.1; LOC100214964.
DR EnsemblMetazoa; XM_012704376.2; XP_012559830.2; LOC100214964.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd09515; SAM_SGMS1-like; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290:SF25; SPHINGOMYELIN SYNTHASE-RELATED PROTEIN 1; 1.
DR PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1.
DR Pfam; PF14360; PAP2_C; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 144..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..80
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
SQ SEQUENCE 436 AA; 50358 MW; C3223FBA88949776 CRC64;
MKNHLAKQKP VHTWTISDVG EWLCKNGFSQ YKELFCDKHK IDGLALITLT IEDLRQPPVQ
IPVLGDIKRI LAKIKTLRSE NSCFDSNASP KGKLNLKKLS VSQSSSSCSD EDEINSFSAD
CTDYVNPRKM SPLEEDMKNA VVSVYFRTFV SFIYMLAVFL LASFTLAVVH DRLPNTSDYP
PLPDVFLEAI PFMPWAFYLC EVCGSIMLFF WCIIIIFHKH RLVVFRRSCA LAGTIFLFRC
FTMYVTSLSV PGKHLDCSPT KYGTFYNRLI RALEIFTGCG MALQGVRTCG DYMFSGHTAT
LTLLNFFVNE YTPRRWYYLH TFCWLLNIFG IFFILAAHEH YSIDVLISFY ITSRLFMYYH
TLASAVQISP SDDRRRRFWF PLFWFFEYGG PLVIKNEFEC LCPTGKCWSV KAKKRLPILV
STFLLNGGLY HINLLF
//