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DG2L6_HUMAN
ID   DG2L6_HUMAN             Reviewed;         337 AA.
AC   Q6ZPD8; Q6IEE2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Diacylglycerol O-acyltransferase 2-like protein 6;
DE            EC=2.3.1.- {ECO:0000269|PubMed:15671038};
DE   AltName: Full=Diacylglycerol O-acyltransferase candidate 3;
DE            Short=hDC3;
GN   Name=DGAT2L6 {ECO:0000312|HGNC:HGNC:23250};
GN   Synonyms=DC3 {ECO:0000303|PubMed:15671038};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Dermoid cancer;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=14970677; DOI=10.1159/000075723;
RA   Winter A., van Eckeveld M., Bininda-Emonds O.R.P., Habermann F.A.,
RA   Fries R.;
RT   "Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus)
RT   and other mammals.";
RL   Cytogenet. Genome Res. 102:42-47(2003).
RN   [4]
RP   CATALYTIC ACTIVITY, LACK OF WAX SYNTHASE ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=15671038; DOI=10.1074/jbc.m500025200;
RA   Turkish A.R., Henneberry A.L., Cromley D., Padamsee M., Oelkers P.,
RA   Bazzi H., Christiano A.M., Billheimer J.T., Sturley S.L.;
RT   "Identification of two novel human Acyl-CoA wax alcohol acyltransferases:
RT   members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily.";
RL   J. Biol. Chem. 280:14755-14764(2005).
RN   [5]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=28420705; DOI=10.1194/jlr.m073445;
RA   Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.;
RT   "Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid
RT   acyltransferases.";
RL   J. Lipid Res. 58:1091-1099(2017).
CC   -!- FUNCTION: Diglyceride acyltransferase that uses fatty acyl-CoA as
CC       substrate (PubMed:15671038). Particularly active with oleate as a
CC       substrate (PubMed:15671038). Has no wax synthase activity to produce
CC       wax esters (PubMed:15671038). Able to use 1-monoalkylglycerol (1-MAkG)
CC       as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol
CC       (MAMAG) (PubMed:28420705). {ECO:0000269|PubMed:15671038,
CC       ECO:0000269|PubMed:28420705}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol =
CC         1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:15671038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-
CC         (9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA;
CC         Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387, ChEBI:CHEBI:138734;
CC         Evidence={ECO:0000269|PubMed:28420705};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC         Evidence={ECO:0000305|PubMed:28420705};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC         (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915,
CC         ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:28420705};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC         Evidence={ECO:0000305|PubMed:28420705};
CC   -!- INTERACTION:
CC       Q6ZPD8; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-12831978, EBI-7131019;
CC       Q6ZPD8; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-12831978, EBI-2813554;
CC       Q6ZPD8; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-12831978, EBI-2876502;
CC       Q6ZPD8; Q13520: AQP6; NbExp=3; IntAct=EBI-12831978, EBI-13059134;
CC       Q6ZPD8; P53365: ARFIP2; NbExp=3; IntAct=EBI-12831978, EBI-638194;
CC       Q6ZPD8; Q12982: BNIP2; NbExp=3; IntAct=EBI-12831978, EBI-752094;
CC       Q6ZPD8; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-12831978, EBI-752069;
CC       Q6ZPD8; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-12831978, EBI-517508;
CC       Q6ZPD8; Q5VYK3: ECPAS; NbExp=3; IntAct=EBI-12831978, EBI-521451;
CC       Q6ZPD8; O95363: FARS2; NbExp=3; IntAct=EBI-12831978, EBI-2513774;
CC       Q6ZPD8; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-12831978, EBI-11959077;
CC       Q6ZPD8; Q05329: GAD2; NbExp=3; IntAct=EBI-12831978, EBI-9304251;
CC       Q6ZPD8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12831978, EBI-13345167;
CC       Q6ZPD8; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-12831978, EBI-1052304;
CC       Q6ZPD8; Q8IX19: MCEMP1; NbExp=3; IntAct=EBI-12831978, EBI-2816356;
CC       Q6ZPD8; Q00013: MPP1; NbExp=3; IntAct=EBI-12831978, EBI-711788;
CC       Q6ZPD8; Q7Z6M4: MTERF4; NbExp=3; IntAct=EBI-12831978, EBI-948435;
CC       Q6ZPD8; Q9HB07: MYG1; NbExp=3; IntAct=EBI-12831978, EBI-709754;
CC       Q6ZPD8; Q9H115: NAPB; NbExp=3; IntAct=EBI-12831978, EBI-3921185;
CC       Q6ZPD8; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-12831978, EBI-11978907;
CC       Q6ZPD8; Q96AL5: PBX3; NbExp=3; IntAct=EBI-12831978, EBI-741171;
CC       Q6ZPD8; O15173: PGRMC2; NbExp=3; IntAct=EBI-12831978, EBI-1050125;
CC       Q6ZPD8; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-12831978, EBI-14223623;
CC       Q6ZPD8; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12831978, EBI-7545592;
CC       Q6ZPD8; P50876: RNF144A; NbExp=3; IntAct=EBI-12831978, EBI-2340657;
CC       Q6ZPD8; Q99942: RNF5; NbExp=3; IntAct=EBI-12831978, EBI-348482;
CC       Q6ZPD8; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-12831978, EBI-8636004;
CC       Q6ZPD8; P57086: SCAND1; NbExp=3; IntAct=EBI-12831978, EBI-745846;
CC       Q6ZPD8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12831978, EBI-17247926;
CC       Q6ZPD8; Q14973: SLC10A1; NbExp=3; IntAct=EBI-12831978, EBI-3923031;
CC       Q6ZPD8; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12831978, EBI-18159983;
CC       Q6ZPD8; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-12831978, EBI-2872322;
CC       Q6ZPD8; O95219: SNX4; NbExp=3; IntAct=EBI-12831978, EBI-724909;
CC       Q6ZPD8; P49675: STAR; NbExp=3; IntAct=EBI-12831978, EBI-722932;
CC       Q6ZPD8; Q8WY91: THAP4; NbExp=3; IntAct=EBI-12831978, EBI-726691;
CC       Q6ZPD8; Q6PL24: TMED8; NbExp=3; IntAct=EBI-12831978, EBI-11603430;
CC       Q6ZPD8; Q96AN5: TMEM143; NbExp=3; IntAct=EBI-12831978, EBI-13342951;
CC       Q6ZPD8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12831978, EBI-8638294;
CC       Q6ZPD8; Q8WV15: TMEM255B; NbExp=3; IntAct=EBI-12831978, EBI-2870087;
CC       Q6ZPD8; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12831978, EBI-6447886;
CC       Q6ZPD8; P49638: TTPA; NbExp=3; IntAct=EBI-12831978, EBI-10210710;
CC       Q6ZPD8; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-12831978, EBI-12261790;
CC       Q6ZPD8; Q9Y4P8-4: WIPI2; NbExp=3; IntAct=EBI-12831978, EBI-12205107;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested except pancreas.
CC       {ECO:0000269|PubMed:15671038}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AK129500; BAC85167.1; -; mRNA.
DR   EMBL; AL139111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL357752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000157; CAD89268.1; -; mRNA.
DR   CCDS; CCDS14397.1; -.
DR   RefSeq; NP_940914.1; NM_198512.2.
DR   AlphaFoldDB; Q6ZPD8; -.
DR   BioGRID; 131445; 49.
DR   IntAct; Q6ZPD8; 43.
DR   STRING; 9606.ENSP00000328036; -.
DR   SwissLipids; SLP:000000305; -.
DR   GlyGen; Q6ZPD8; 1 site, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; Q6ZPD8; -.
DR   BioMuta; DGAT2L6; -.
DR   DMDM; 74749597; -.
DR   MassIVE; Q6ZPD8; -.
DR   PaxDb; Q6ZPD8; -.
DR   PeptideAtlas; Q6ZPD8; -.
DR   PRIDE; Q6ZPD8; -.
DR   Antibodypedia; 13248; 44 antibodies from 17 providers.
DR   DNASU; 347516; -.
DR   Ensembl; ENST00000333026.4; ENSP00000328036.3; ENSG00000184210.6.
DR   GeneID; 347516; -.
DR   KEGG; hsa:347516; -.
DR   MANE-Select; ENST00000333026.4; ENSP00000328036.3; NM_198512.3; NP_940914.1.
DR   UCSC; uc004dxx.2; human.
DR   CTD; 347516; -.
DR   DisGeNET; 347516; -.
DR   GeneCards; DGAT2L6; -.
DR   HGNC; HGNC:23250; DGAT2L6.
DR   HPA; ENSG00000184210; Group enriched (breast, skin).
DR   MIM; 300926; gene.
DR   neXtProt; NX_Q6ZPD8; -.
DR   OpenTargets; ENSG00000184210; -.
DR   PharmGKB; PA143485448; -.
DR   VEuPathDB; HostDB:ENSG00000184210; -.
DR   eggNOG; KOG0831; Eukaryota.
DR   GeneTree; ENSGT01030000234582; -.
DR   HOGENOM; CLU_023995_0_0_1; -.
DR   InParanoid; Q6ZPD8; -.
DR   OMA; GTWIRFF; -.
DR   OrthoDB; 1347007at2759; -.
DR   PhylomeDB; Q6ZPD8; -.
DR   TreeFam; TF314707; -.
DR   BRENDA; 2.3.1.20; 2681.
DR   BRENDA; 2.3.1.75; 2681.
DR   PathwayCommons; Q6ZPD8; -.
DR   Reactome; R-HSA-1482883; Acyl chain remodeling of DAG and TAG.
DR   SignaLink; Q6ZPD8; -.
DR   BioGRID-ORCS; 347516; 6 hits in 688 CRISPR screens.
DR   GenomeRNAi; 347516; -.
DR   Pharos; Q6ZPD8; Tbio.
DR   PRO; PR:Q6ZPD8; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q6ZPD8; protein.
DR   Bgee; ENSG00000184210; Expressed in sural nerve and 9 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; EXP:Reactome.
DR   GO; GO:0036155; P:acylglycerol acyl-chain remodeling; TAS:Reactome.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0006640; P:monoacylglycerol biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR007130; DAGAT.
DR   Pfam; PF03982; DAGAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..337
FT                   /note="Diacylglycerol O-acyltransferase 2-like protein 6"
FT                   /id="PRO_0000249054"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   337 AA;  38593 MW;  E14B50FBD01981E4 CRC64;
     MAFFSRLNLQ EGLQTFFVLQ WIPVYIFLGA IPILLIPYFL LFSKFWPLAV LSLAWLTYDW
     NTHSQGGRRS AWVRNWTLWK YFRNYFPVKL VKTHDLSPKH NYIIANHPHG ILSFGVFINF
     ATEATGIARI FPSITPFVGT LERIFWIPIV REYVMSMGVC PVSSSALKYL LTQKGSGNAV
     VIVVGGAAEA LLCRPGASTL FLKQRKGFVK MALQTGAYLV PSYSFGENEV FNQETFPEGT
     WLRLFQKTFQ DTFKKILGLN FCTFHGRGFT RGSWGFLPFN RPITTVVGEP LPIPRIKRPN
     QKTVDKYHAL YISALRKLFD QHKVEYGLPE TQELTIT
 
 
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