ID   SESD1_MOUSE             Reviewed;         696 AA.
AC   Q80UK0; Q3TLJ1; Q810W3; Q8CI09;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=SEC14 domain and spectrin repeat-containing protein 1;
DE   AltName: Full=Huntingtin-interacting protein-like protein;
GN   Name=Sestd1;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 498-696.
RC   TISSUE=Mammary gland;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
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).
CC   -!- FUNCTION: May act as the primary docking protein directing membrane
CC       turnover and assembly of the transient receptor potential channels
CC       TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol
CC       monophosphates, phosphatidylinositol diphosphates (PIP2s) and
CC       phosphatidic acid, but not less polar lipids including
CC       phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The
CC       binding to PIP2s is calcium dependent. Might be involved in the plasma
CC       membrane localization of CTNNB1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via the spectrin 1 repeat) with TRPC4 and TRPC5
CC       (via CIRB domain). Interacts with CTNNB1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SOLO family. {ECO:0000305}.
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DR   EMBL; AL772242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038005; AAH38005.1; -; mRNA.
DR   EMBL; BC044853; AAH44853.1; -; mRNA.
DR   EMBL; BC048358; AAH48358.1; -; mRNA.
DR   EMBL; AK166483; BAE38801.1; -; mRNA.
DR   CCDS; CCDS16163.1; -.
DR   RefSeq; NP_780674.1; NM_175465.6.
DR   RefSeq; XP_006499263.1; XM_006499200.2.
DR   RefSeq; XP_006499264.1; XM_006499201.2.
DR   RefSeq; XP_006499265.1; XM_006499202.3.
DR   AlphaFoldDB; Q80UK0; -.
DR   SMR; Q80UK0; -.
DR   BioGRID; 230712; 6.
DR   IntAct; Q80UK0; 7.
DR   STRING; 10090.ENSMUSP00000099720; -.
DR   iPTMnet; Q80UK0; -.
DR   PhosphoSitePlus; Q80UK0; -.
DR   EPD; Q80UK0; -.
DR   MaxQB; Q80UK0; -.
DR   PaxDb; Q80UK0; -.
DR   PeptideAtlas; Q80UK0; -.
DR   PRIDE; Q80UK0; -.
DR   ProteomicsDB; 255392; -.
DR   Antibodypedia; 47625; 127 antibodies from 23 providers.
DR   DNASU; 228071; -.
DR   Ensembl; ENSMUST00000102659; ENSMUSP00000099720; ENSMUSG00000042272.
DR   Ensembl; ENSMUST00000102660; ENSMUSP00000099721; ENSMUSG00000042272.
DR   GeneID; 228071; -.
DR   KEGG; mmu:228071; -.
DR   UCSC; uc008kfx.3; mouse.
DR   CTD; 91404; -.
DR   MGI; MGI:1916262; Sestd1.
DR   VEuPathDB; HostDB:ENSMUSG00000042272; -.
DR   eggNOG; KOG4240; Eukaryota.
DR   GeneTree; ENSGT00730000111148; -.
DR   HOGENOM; CLU_010440_1_0_1; -.
DR   InParanoid; Q80UK0; -.
DR   OMA; SMDLNFL; -.
DR   OrthoDB; 230255at2759; -.
DR   PhylomeDB; Q80UK0; -.
DR   TreeFam; TF332003; -.
DR   BioGRID-ORCS; 228071; 3 hits in 69 CRISPR screens.
DR   ChiTaRS; Sestd1; mouse.
DR   PRO; PR:Q80UK0; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q80UK0; protein.
DR   Bgee; ENSMUSG00000042272; Expressed in otolith organ and 229 other tissues.
DR   Genevisible; Q80UK0; MM.
DR   GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR   GO; GO:0070300; F:phosphatidic acid binding; ISO:MGI.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:MGI.
DR   GO; GO:1904878; P:negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI.
DR   CDD; cd00170; SEC14; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Repeat.
FT   CHAIN           1..696
FT                   /note="SEC14 domain and spectrin repeat-containing protein
FT                   1"
FT                   /id="PRO_0000309480"
FT   DOMAIN          1..153
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REPEAT          275..378
FT                   /note="Spectrin 1"
FT   REPEAT          381..494
FT                   /note="Spectrin 2"
FT   REPEAT          500..602
FT                   /note="Spectrin 3"
FT   CONFLICT        480..482
FT                   /note="QRC -> HAS (in Ref. 1; AAH38005)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   696 AA;  79376 MW;  8354593E717D73F4 CRC64;
     MEASVILPIL KKKLAFLSGG KDRRSGLILT IPLCLEQTSM DELSVTLDYL LSIPSEKCKA
     RGFTVIVDGR KSQWNVVKTV VLMLQNVVPA EVSLVCVVKP DEFWDKKVTH FCFWKEKDRL
     GFEVILVSAN KLTRYIEPCQ LTEDFGGSLT YDHMDWLNKR LVFEKFTKES TSLLDELALI
     NNGSDKGNEQ EKERSVDLNF LPSVDPETVL QTGHELLSEL QQRRFNGSDG GVSWSPMDDE
     LLAQPQVMKL LDSLREQYTR YQEVCRQRSK RTQLEEIQQK VMQVVNWLEG PGSEQLRAQW
     GIGDSIRASQ ALQQKHEEIE SQHSEWFAVY VELNQQIAAL LNAGDEEDLV ELKSLQQQLS
     DVCYRQASQL EFRQNLLQAA LEFHGVAQDL SQQLDGLLGM LCVDVAPADG ASIQQTLKLL
     EEKLKSVDVG LQGLREKGQG LLDQISNQAS WAYGKDVTIE NKENVDHIQG VMEDMQLRKQ
     RCEDMVDVRR LKMLQMVQLF KCEEDASQAV EWLSELLDAL LKTHIRLGDD AQETKVLLEK
     HRKFVDVAQS TYDYGRQLLQ ATVVLCQSLR CTSRSSGDTL PRLNRVWKQF TVASEERVHR
     LEMAIAFHSN AEKILQDCPE EPEAMNDEEQ FEEIEAIGKS LLDRLTIPVV YPDGTEQYFG
     SPSDMASTAE HIRDRMKLVS LKRQQLRHPE LVTTES