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Protein

SEC14 domain and spectrin repeat-containing protein 1

Gene

SESTD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1.1 Publication

GO - Molecular functioni

  1. phosphatidic acid binding Source: UniProtKB
  2. phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
  3. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
  4. phosphatidylinositol-3-phosphate binding Source: UniProtKB
  5. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  6. phosphatidylinositol-4-phosphate binding Source: UniProtKB
  7. phosphatidylinositol-5-phosphate binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SEC14 domain and spectrin repeat-containing protein 1
Alternative name(s):
Huntingtin-interacting protein-like protein
Protein Solo
Gene namesi
Name:SESTD1
Synonyms:SOLO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18379. SESTD1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38534.

Polymorphism and mutation databases

BioMutaiSESTD1.
DMDMi160358740.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 696696SEC14 domain and spectrin repeat-containing protein 1PRO_0000309479Add
BLAST

Proteomic databases

MaxQBiQ86VW0.
PaxDbiQ86VW0.
PRIDEiQ86VW0.

PTM databases

PhosphoSiteiQ86VW0.

Expressioni

Tissue specificityi

Broad expression. High expression in thalamus and brain. Significantly expressed in vasculature.1 Publication

Gene expression databases

BgeeiQ86VW0.
CleanExiHS_SESTD1.
ExpressionAtlasiQ86VW0. baseline and differential.
GenevestigatoriQ86VW0.

Interactioni

Subunit structurei

Interacts (via the spectrin 1 repeat) with TRPC4 and TRPC5 (via CIRB domain). Interacts with CTNNB1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GPS2Q132273EBI-6117072,EBI-713355
STMN1P169493EBI-6117072,EBI-445909
STMN1Q96CE43EBI-6117072,EBI-10283192

Protein-protein interaction databases

BioGridi124826. 7 interactions.
IntActiQ86VW0. 7 interactions.
MINTiMINT-4875522.
STRINGi9606.ENSP00000415332.

Structurei

3D structure databases

ProteinModelPortaliQ86VW0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 153153CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST
Repeati275 – 378104Spectrin 1Add
BLAST
Repeati381 – 494114Spectrin 2Add
BLAST
Repeati500 – 602103Spectrin 3Add
BLAST

Sequence similaritiesi

Belongs to the SOLO family.Curated
Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
Contains 3 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149526.
GeneTreeiENSGT00730000111148.
HOGENOMiHOG000072717.
HOVERGENiHBG104429.
InParanoidiQ86VW0.
OMAiCPMEEEL.
OrthoDBiEOG7D59MS.
PhylomeDBiQ86VW0.
TreeFamiTF332003.

Family and domain databases

InterProiIPR001251. CRAL-TRIO_dom.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PfamiPF13716. CRAL_TRIO_2. 1 hit.
[Graphical view]
SMARTiSM00150. SPEC. 2 hits.
[Graphical view]
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86VW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEASVILPIL KKKLAFLSGG KDRRSGLILT IPLCLEQTNM DELSVTLDYL
60 70 80 90 100
LSIPSEKCKA RGFTVIVDGR KSQWNVVKTV VVMLQNVVPA EVSLVCVVKP
110 120 130 140 150
DEFWDKKVTH FCFWKEKDRL GFEVILVSAN KLTRYIEPCQ LTEDFGGSLT
160 170 180 190 200
YDHMDWLNKR LVFEKFTKES TSLLDELALI NNGSDKGNQQ EKERSVDLNF
210 220 230 240 250
LPSVDPETVL QTGHELLSEL QQRRFNGSDG GVSWSPMDDE LLAQPQVMKL
260 270 280 290 300
LDSLREQYTR YQEVCRQRSK RTQLEEIQQK VMQVVNWLEG PGSEQLRAQW
310 320 330 340 350
GIGDSIRASQ ALQQKHEEIE SQHSEWFAVY VELNQQIAAL LNAGDEEDLV
360 370 380 390 400
ELKSLQQQLS DVCYRQASQL EFRQNLLQAA LEFHGVAQDL SQQLDGLLGM
410 420 430 440 450
LCVDVAPADG ASIQQTLKLL EEKLKSVDVG LQGLREKGQG LLDQISNQAS
460 470 480 490 500
WAYGKDVTIE NKENVDHIQG VMEDMQLRKQ RCEDMVDVRR LKMLQMVQLF
510 520 530 540 550
KCEEDAAQAV EWLSELLDAL LKTHIRLGDD AQETKVLLEK HRKFVDVAQS
560 570 580 590 600
TYDYGRQLLQ ATVVLCQSLR CTSRSSGDTL PRLNRVWKQF TIASEERVHR
610 620 630 640 650
LEMAIAFHSN AEKILQDCPE EPEAINDEEQ FDEIEAVGKS LLDRLTVPVV
660 670 680 690
YPDGTEQYFG SPSDMASTAE NIRDRMKLVN LKRQQLRHPE MVTTES
Length:696
Mass (Da):79,348
Last modified:November 13, 2007 - v2
Checksum:i5C5C80EB57A7303A
GO

Sequence cautioni

The sequence BAB71618.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti508 – 5081Q → H in AAP47744 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491Y → F.1 Publication
Corresponds to variant rs17854501 [ dbSNP | Ensembl ].
VAR_036963
Natural varianti563 – 5631V → A.
Corresponds to variant rs1047994 [ dbSNP | Ensembl ].
VAR_051919

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY209190 mRNA. Translation: AAP47744.1.
AC016755 Genomic DNA. Translation: AAY24323.1.
AC093911 Genomic DNA. Translation: AAY24093.1.
BC029744 mRNA. Translation: AAH29744.1.
BC047578 mRNA. Translation: AAH47578.1.
AK057944 mRNA. Translation: BAB71618.1. Different initiation.
CCDSiCCDS33338.1.
PIRiT34530.
RefSeqiNP_835224.3. NM_178123.4.
UniGeneiHs.30977.

Genome annotation databases

EnsembliENST00000428443; ENSP00000415332; ENSG00000187231.
GeneIDi91404.
KEGGihsa:91404.
UCSCiuc002uni.4. human.

Polymorphism and mutation databases

BioMutaiSESTD1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY209190 mRNA. Translation: AAP47744.1.
AC016755 Genomic DNA. Translation: AAY24323.1.
AC093911 Genomic DNA. Translation: AAY24093.1.
BC029744 mRNA. Translation: AAH29744.1.
BC047578 mRNA. Translation: AAH47578.1.
AK057944 mRNA. Translation: BAB71618.1. Different initiation.
CCDSiCCDS33338.1.
PIRiT34530.
RefSeqiNP_835224.3. NM_178123.4.
UniGeneiHs.30977.

3D structure databases

ProteinModelPortaliQ86VW0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124826. 7 interactions.
IntActiQ86VW0. 7 interactions.
MINTiMINT-4875522.
STRINGi9606.ENSP00000415332.

PTM databases

PhosphoSiteiQ86VW0.

Polymorphism and mutation databases

BioMutaiSESTD1.
DMDMi160358740.

Proteomic databases

MaxQBiQ86VW0.
PaxDbiQ86VW0.
PRIDEiQ86VW0.

Protocols and materials databases

DNASUi91404.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000428443; ENSP00000415332; ENSG00000187231.
GeneIDi91404.
KEGGihsa:91404.
UCSCiuc002uni.4. human.

Organism-specific databases

CTDi91404.
GeneCardsiGC02M179966.
H-InvDBHIX0002639.
HGNCiHGNC:18379. SESTD1.
neXtProtiNX_Q86VW0.
PharmGKBiPA38534.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149526.
GeneTreeiENSGT00730000111148.
HOGENOMiHOG000072717.
HOVERGENiHBG104429.
InParanoidiQ86VW0.
OMAiCPMEEEL.
OrthoDBiEOG7D59MS.
PhylomeDBiQ86VW0.
TreeFamiTF332003.

Miscellaneous databases

ChiTaRSiSESTD1. human.
GeneWikiiSESTD1.
GenomeRNAii91404.
NextBioi77223.
PROiQ86VW0.

Gene expression databases

BgeeiQ86VW0.
CleanExiHS_SESTD1.
ExpressionAtlasiQ86VW0. baseline and differential.
GenevestigatoriQ86VW0.

Family and domain databases

InterProiIPR001251. CRAL-TRIO_dom.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PfamiPF13716. CRAL_TRIO_2. 1 hit.
[Graphical view]
SMARTiSM00150. SPEC. 2 hits.
[Graphical view]
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Xu J., Xie Y., Mao Y.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-49.
    Tissue: Brain and Urinary bladder.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-696.
  5. "The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5."
    Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.
    J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRPC4; TRPC5 AND CTNNB1, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSESD1_HUMAN
AccessioniPrimary (citable) accession number: Q86VW0
Secondary accession number(s): Q53R38
, Q53SP3, Q5GM69, Q8N6M1, Q96LQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: April 29, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Called SOLO because the encoded protein is related to but shorter than DUO and TRIO.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.