ID A0A024R3P1_HUMAN Unreviewed; 323 AA. AC A0A024R3P1; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-APR-2021, entry version 44. DE RecName: Full=Degenerative spermatocyte homolog 1 {ECO:0000256|ARBA:ARBA00023861}; DE EC=1.14.19.17 {ECO:0000256|ARBA:ARBA00012021}; DE AltName: Full=Dihydroceramide desaturase-1 {ECO:0000256|ARBA:ARBA00023903}; DE AltName: Full=Sphingolipid delta(4)-desaturase DES1 {ECO:0000256|ARBA:ARBA00023815}; GN Name=DEGS1 {ECO:0000313|EMBL:EAW69712.1}; GN ORFNames=hCG_1736748 {ECO:0000313|EMBL:EAW69712.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:EAW69712.1}; RN [1] {ECO:0000313|EMBL:EAW69712.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:EAW69712.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=11-cis-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55356, CC ChEBI:CHEBI:16302, ChEBI:CHEBI:45479; CC Evidence={ECO:0000256|ARBA:ARBA00023728}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55357; CC Evidence={ECO:0000256|ARBA:ARBA00023728}; CC -!- CATALYTIC ACTIVITY: CC Reaction=11-cis-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55360, CC ChEBI:CHEBI:16302, ChEBI:CHEBI:78272; CC Evidence={ECO:0000256|ARBA:ARBA00023689}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55361; CC Evidence={ECO:0000256|ARBA:ARBA00023689}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 [Fe(II)-cytochrome b5] + an N-acylsphinganine + 2 H(+) + O2 CC = 2 [Fe(III)-cytochrome b5] + an N-acylsphing-4-enine + 2 H2O; CC Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488, CC ChEBI:CHEBI:52639; EC=1.14.19.17; CC Evidence={ECO:0000256|ARBA:ARBA00023713}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + an N-acylsphinganine + O2 = A + an N-acylsphing-4-enine CC + 2 H2O; Xref=Rhea:RHEA:36075, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:31488, CC ChEBI:CHEBI:52639; Evidence={ECO:0000256|ARBA:ARBA00023731}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36076; CC Evidence={ECO:0000256|ARBA:ARBA00023731}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinol = 11-cis-retinol; Xref=Rhea:RHEA:19141, CC ChEBI:CHEBI:16302, ChEBI:CHEBI:17336; CC Evidence={ECO:0000256|ARBA:ARBA00023720}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19142; CC Evidence={ECO:0000256|ARBA:ARBA00023720}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19143; CC Evidence={ECO:0000256|ARBA:ARBA00023720}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55352, CC ChEBI:CHEBI:17336, ChEBI:CHEBI:45479; CC Evidence={ECO:0000256|ARBA:ARBA00023714}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55353; CC Evidence={ECO:0000256|ARBA:ARBA00023714}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55348, CC ChEBI:CHEBI:17336, ChEBI:CHEBI:78272; CC Evidence={ECO:0000256|ARBA:ARBA00023675}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55349; CC Evidence={ECO:0000256|ARBA:ARBA00023675}; CC -!- SUBUNIT: Interacts with RLBP1; the interaction increases synthesis of CC chromophore-precursors by DEGS1. {ECO:0000256|ARBA:ARBA00023795}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|PIRNR:PIRNR017228}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004325}. CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS CC subfamily. {ECO:0000256|ARBA:ARBA00006146, CC ECO:0000256|PIRNR:PIRNR017228}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH471098; EAW69712.1; -; Genomic_DNA. DR RefSeq; NP_003667.1; NM_003676.3. DR BindingDB; A0A024R3P1; -. DR Antibodypedia; 20751; 164 antibodies. DR DNASU; 8560; -. DR GeneID; 8560; -. DR KEGG; hsa:8560; -. DR CTD; 8560; -. DR VEuPathDB; HostDB:ENSG00000143753.12; -. DR OMA; FTYIHLL; -. DR OrthoDB; 1255438at2759; -. DR PhylomeDB; A0A024R3P1; -. DR BioGRID-ORCS; 8560; 9 hits in 996 CRISPR screens. DR ChiTaRS; DEGS1; human. DR GenomeRNAi; 8560; -. DR Bgee; ENSG00000143753; Expressed in penis and 245 other tissues. DR ExpressionAtlas; A0A024R3P1; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0050251; F:retinol isomerase activity; IEA:RHEA. DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro. DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1. DR InterPro; IPR031196; DES1. DR InterPro; IPR011388; DES1/DES2. DR InterPro; IPR005804; FA_desaturase_dom. DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N. DR PANTHER; PTHR12879:SF2; PTHR12879:SF2; 1. DR Pfam; PF00487; FA_desaturase; 1. DR Pfam; PF08557; Lipid_DES; 1. DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1. DR SMART; SM01269; Lipid_DES; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR017228}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, KW ECO:0000256|PIRNR:PIRNR017228}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|PIRNR:PIRNR017228}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707}; KW Membrane {ECO:0000256|PIRNR:PIRNR017228, ECO:0000256|SAM:Phobius}; KW Myristate {ECO:0000256|ARBA:ARBA00022707}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR017228}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43..62 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 68..92 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 104..122 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 150..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 184..204 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 210..231 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 5..43 FT /note="Lipid_DES" FT /evidence="ECO:0000259|SMART:SM01269" SQ SEQUENCE 323 AA; 37866 MW; 9FF2E4A0B87EA71C CRC64; MGSRVSREDF EWVYTDQPHA DRRREILAKY PEIKSLMKPD PNLIWIIIMM VLTQLGAFYI VKDLDWKWVI FGAYAFGSCI NHSMTLAIHE IAHNAAFGNC KAMWNRWFGM FANLPIGIPY SISFKRYHMD HHRYLGADGV DVDIPTDFEG WFFCTAFRKF IWVILQPLFY AFRPLFINPK PITYLEVINT VAQVTFDILI YYFLGIKSLV YMLAASLLGL GLHPISGHFI AEHYMFLKGH ETYSYYGPLN LLTFNVGYHN EHHDFPNIPG KSLPLVRKIA AEYYDNLPHY NSWIKVLYDF VMDDTISPYS RMKRHQKGEM VLE //