ID   SESD1_HUMAN             Reviewed;         696 AA.
AC   Q86VW0; Q53R38; Q53SP3; Q5GM69; Q8N6M1; Q96LQ2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=SEC14 domain and spectrin repeat-containing protein 1;
DE   AltName: Full=Huntingtin-interacting protein-like protein;
DE   AltName: Full=Protein Solo;
GN   Name=SESTD1; Synonyms=SOLO;
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 [MRNA].
RA   Xu J., Xie Y., Mao Y.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-49.
RC   TISSUE=Brain, and Urinary bladder;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-696.
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   [5]
RP   FUNCTION, INTERACTION WITH TRPC4; TRPC5 AND CTNNB1, AND TISSUE SPECIFICITY.
RX   PubMed=20164195; DOI=10.1074/jbc.m109.068304;
RA   Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.;
RT   "The phospholipid-binding protein SESTD1 is a novel regulator of the
RT   transient receptor potential channels TRPC4 and TRPC5.";
RL   J. Biol. Chem. 285:12426-12434(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. {ECO:0000269|PubMed:20164195}.
CC   -!- SUBUNIT: Interacts (via the spectrin 1 repeat) with TRPC4 and TRPC5
CC       (via CIRB domain). Interacts with CTNNB1.
CC       {ECO:0000269|PubMed:20164195}.
CC   -!- INTERACTION:
CC       Q86VW0; Q9HC52: CBX8; NbExp=3; IntAct=EBI-6117072, EBI-712912;
CC       Q86VW0; G5E9H6: DACT3; NbExp=3; IntAct=EBI-6117072, EBI-12296095;
CC       Q86VW0; Q13227: GPS2; NbExp=7; IntAct=EBI-6117072, EBI-713355;
CC       Q86VW0; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-6117072, EBI-12056251;
CC       Q86VW0; Q15051-2: IQCB1; NbExp=3; IntAct=EBI-6117072, EBI-11944935;
CC       Q86VW0; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-6117072, EBI-14093916;
CC       Q86VW0; P16949: STMN1; NbExp=3; IntAct=EBI-6117072, EBI-445909;
CC       Q86VW0; Q96CE4: STMN1; NbExp=3; IntAct=EBI-6117072, EBI-10283192;
CC       Q86VW0; Q93045: STMN2; NbExp=3; IntAct=EBI-6117072, EBI-714194;
CC       Q86VW0; Q15561: TEAD4; NbExp=3; IntAct=EBI-6117072, EBI-747736;
CC       Q86VW0; Q96NB3: ZNF830; NbExp=3; IntAct=EBI-6117072, EBI-3920997;
CC   -!- TISSUE SPECIFICITY: Broad expression. High expression in thalamus and
CC       brain. Significantly expressed in vasculature.
CC       {ECO:0000269|PubMed:20164195}.
CC   -!- MISCELLANEOUS: Called SOLO because the encoded protein is related to
CC       but shorter than DUO and TRIO.
CC   -!- SIMILARITY: Belongs to the SOLO family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71618.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY209190; AAP47744.1; -; mRNA.
DR   EMBL; AC016755; AAY24323.1; -; Genomic_DNA.
DR   EMBL; AC093911; AAY24093.1; -; Genomic_DNA.
DR   EMBL; BC029744; AAH29744.1; -; mRNA.
DR   EMBL; BC047578; AAH47578.1; -; mRNA.
DR   EMBL; AK057944; BAB71618.1; ALT_INIT; mRNA.
DR   CCDS; CCDS33338.1; -.
DR   PIR; T34530; T34530.
DR   RefSeq; NP_835224.3; NM_178123.4.
DR   RefSeq; XP_011510441.1; XM_011512139.2.
DR   AlphaFoldDB; Q86VW0; -.
DR   SMR; Q86VW0; -.
DR   BioGRID; 124826; 31.
DR   IntAct; Q86VW0; 28.
DR   STRING; 9606.ENSP00000415332; -.
DR   SwissLipids; SLP:000001538; -.
DR   iPTMnet; Q86VW0; -.
DR   PhosphoSitePlus; Q86VW0; -.
DR   BioMuta; SESTD1; -.
DR   DMDM; 160358740; -.
DR   EPD; Q86VW0; -.
DR   jPOST; Q86VW0; -.
DR   MassIVE; Q86VW0; -.
DR   MaxQB; Q86VW0; -.
DR   PaxDb; 9606-ENSP00000415332; -.
DR   PeptideAtlas; Q86VW0; -.
DR   ProteomicsDB; 70078; -.
DR   Pumba; Q86VW0; -.
DR   Antibodypedia; 47625; 149 antibodies from 23 providers.
DR   DNASU; 91404; -.
DR   Ensembl; ENST00000428443.8; ENSP00000415332.2; ENSG00000187231.14.
DR   GeneID; 91404; -.
DR   KEGG; hsa:91404; -.
DR   MANE-Select; ENST00000428443.8; ENSP00000415332.2; NM_178123.5; NP_835224.3.
DR   UCSC; uc002uni.5; human.
DR   AGR; HGNC:18379; -.
DR   CTD; 91404; -.
DR   DisGeNET; 91404; -.
DR   GeneCards; SESTD1; -.
DR   HGNC; HGNC:18379; SESTD1.
DR   HPA; ENSG00000187231; Low tissue specificity.
DR   neXtProt; NX_Q86VW0; -.
DR   OpenTargets; ENSG00000187231; -.
DR   PharmGKB; PA38534; -.
DR   VEuPathDB; HostDB:ENSG00000187231; -.
DR   eggNOG; KOG4240; Eukaryota.
DR   GeneTree; ENSGT00730000111148; -.
DR   HOGENOM; CLU_010440_1_0_1; -.
DR   InParanoid; Q86VW0; -.
DR   OMA; PDAFWDK; -.
DR   OrthoDB; 2878608at2759; -.
DR   PhylomeDB; Q86VW0; -.
DR   TreeFam; TF332003; -.
DR   PathwayCommons; Q86VW0; -.
DR   SignaLink; Q86VW0; -.
DR   BioGRID-ORCS; 91404; 10 hits in 1152 CRISPR screens.
DR   ChiTaRS; SESTD1; human.
DR   GeneWiki; SESTD1; -.
DR   GenomeRNAi; 91404; -.
DR   Pharos; Q86VW0; Tbio.
DR   PRO; PR:Q86VW0; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q86VW0; Protein.
DR   Bgee; ENSG00000187231; Expressed in calcaneal tendon and 188 other cell types or tissues.
DR   ExpressionAtlas; Q86VW0; baseline and differential.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
DR   GO; GO:1904878; P:negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IMP:UniProtKB.
DR   Gene3D; 1.20.58.60; -; 2.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   PANTHER; PTHR46607; SEC14 DOMAIN AND SPECTRIN REPEAT-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46607:SF1; SEC14 DOMAIN AND SPECTRIN REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   Genevisible; Q86VW0; HS.
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_0000309479"
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   VARIANT         49
FT                   /note="Y -> F (in dbSNP:rs17854501)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_036963"
FT   VARIANT         563
FT                   /note="V -> A (in dbSNP:rs1047994)"
FT                   /id="VAR_051919"
FT   CONFLICT        508
FT                   /note="Q -> H (in Ref. 1; AAP47744)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   696 AA;  79348 MW;  5C5C80EB57A7303A CRC64;
     MEASVILPIL KKKLAFLSGG KDRRSGLILT IPLCLEQTNM DELSVTLDYL LSIPSEKCKA
     RGFTVIVDGR KSQWNVVKTV VVMLQNVVPA EVSLVCVVKP DEFWDKKVTH FCFWKEKDRL
     GFEVILVSAN KLTRYIEPCQ LTEDFGGSLT YDHMDWLNKR LVFEKFTKES TSLLDELALI
     NNGSDKGNQQ 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 KCEEDAAQAV EWLSELLDAL LKTHIRLGDD AQETKVLLEK
     HRKFVDVAQS TYDYGRQLLQ ATVVLCQSLR CTSRSSGDTL PRLNRVWKQF TIASEERVHR
     LEMAIAFHSN AEKILQDCPE EPEAINDEEQ FDEIEAVGKS LLDRLTVPVV YPDGTEQYFG
     SPSDMASTAE NIRDRMKLVN LKRQQLRHPE MVTTES
//