TECRL_MOUSE
ID TECRL_MOUSE Reviewed; 361 AA.
AC Q8BFZ1; Q8CIX3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Trans-2,3-enoyl-CoA reductase-like;
DE EC=1.3.1.-;
DE AltName: Full=Steroid 5-alpha-reductase 2-like 2 protein;
GN Name=Tecrl; Synonyms=Srd5a2l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Chen X.-G., Yong L., Zhang D.-L., Cheng J., Zhu W.-L., Dao J.-J.;
RT "Molecular cloning and expression analysis of Srd5a2l2, a novel mouse
RT member of steroid 5 alpha-reductase family.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 30:894-899(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-35, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27861123; DOI=10.15252/emmm.201505719;
RA Devalla H.D., Gelinas R., Aburawi E.H., Beqqali A., Goyette P., Freund C.,
RA Chaix M.A., Tadros R., Jiang H., Le Bechec A., Monshouwer-Kloots J.J.,
RA Zwetsloot T., Kosmidis G., Latour F., Alikashani A., Hoekstra M.,
RA Schlaepfer J., Mummery C.L., Stevenson B., Kutalik Z., de Vries A.A.,
RA Rivard L., Wilde A.A., Talajic M., Verkerk A.O., Al-Gazali L., Rioux J.D.,
RA Bhuiyan Z.A., Passier R.;
RT "TECRL, a new life-threatening inherited arrhythmia gene associated with
RT overlapping clinical features of both LQTS and CPVT.";
RL EMBO Mol. Med. 8:1390-1408(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q5HYJ1}.
CC -!- TISSUE SPECIFICITY: Expression is highest in the heart with very low to
CC almost undetectable levels in brain, skeletal muscle, stomach,
CC pancreas, liver, kidney, small intestine, and uterus.
CC {ECO:0000269|PubMed:27861123}.
CC -!- DEVELOPMENTAL STAGE: At embryonic day 8.5 dpc, expressed in the
CC developing heart with the strongest expression occurring in the inflow
CC tract, especially in the left horn. At 9.5 dpc, expression is still
CC detectable in the atria and ventricles, albeit at lower levels whereas
CC strong expression remains in the inflow tract. From 10 dpc onwards, it
CC is also expressed at low levels in somites, particularly in the myotome
CC region, that gives rise to skeletal muscle. At 10.5 dpc, cardiac
CC expression is no longer restricted to the inflow tract. At 14.5 dpc, it
CC is expressed in the entire myocardium. {ECO:0000269|PubMed:27861123}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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; AF548365; AAN40798.1; -; mRNA.
DR EMBL; AK052276; BAC34913.1; -; mRNA.
DR EMBL; AK052284; BAC34916.1; -; mRNA.
DR EMBL; BC107366; AAI07367.1; -; mRNA.
DR EMBL; BC107367; AAI07368.1; -; mRNA.
DR CCDS; CCDS19375.1; -.
DR RefSeq; NP_722496.2; NM_153801.3.
DR AlphaFoldDB; Q8BFZ1; -.
DR SMR; Q8BFZ1; -.
DR STRING; 10090.ENSMUSP00000062122; -.
DR iPTMnet; Q8BFZ1; -.
DR PhosphoSitePlus; Q8BFZ1; -.
DR PaxDb; Q8BFZ1; -.
DR PRIDE; Q8BFZ1; -.
DR ProteomicsDB; 263099; -.
DR Antibodypedia; 68497; 79 antibodies from 12 providers.
DR DNASU; 243078; -.
DR Ensembl; ENSMUST00000053543; ENSMUSP00000062122; ENSMUSG00000049537.
DR GeneID; 243078; -.
DR KEGG; mmu:243078; -.
DR UCSC; uc008xwu.2; mouse.
DR CTD; 253017; -.
DR MGI; MGI:2444966; Tecrl.
DR VEuPathDB; HostDB:ENSMUSG00000049537; -.
DR eggNOG; KOG1639; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_059260_1_0_1; -.
DR InParanoid; Q8BFZ1; -.
DR OMA; RQVSWTT; -.
DR OrthoDB; 720263at2759; -.
DR PhylomeDB; Q8BFZ1; -.
DR TreeFam; TF300908; -.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 243078; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8BFZ1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BFZ1; protein.
DR Bgee; ENSMUSG00000049537; Expressed in myocardium of ventricle and 47 other tissues.
DR ExpressionAtlas; Q8BFZ1; baseline and differential.
DR Genevisible; Q8BFZ1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="Trans-2,3-enoyl-CoA reductase-like"
FT /id="PRO_0000317714"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 232
FT /note="Y -> H (in Ref. 1; AAN40798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41893 MW; DBE3D7C080A82113 CRC64;
MFKRHKSLER KRELLFQGLP QSTMKNNARN FHSLSQLVLS AGPLKTTTAV KHSKTTHFEI
EILDAHTRKQ ICIVDKVTQT STIHDVKQKF HKACPKWYPS RIGLQLEYGG PYLRDYITVQ
SVAASSIITL YFTDLGQQVG WTTVFLAEYS GPLLIYLLFY LRSSYIYDVK ESTRWPRHPV
VHLAFFCHCI HYIRLLLETL FVHKVSTGHS PMKNLIKGCA FYWGFTSWMA YYINHPRYTP
PSFGNRQVIV SAINFLFCEA GNHFINTVLA HPNHTGSNAC FPSPNYNPFT WLFFLVSCPN
YTYEIGSWIS FTVMTQTLPV GIFTILMTIQ MSLWARKKHK IYRKKFNSYV HRKSAIIPLI
L
