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Syntaxin-16 (Syn16)

 STX16_HUMAN             Reviewed;         325 AA.
O14662; A6NK32; A6NN69; A8MPP0; B7ZBN1; B7ZBN2; B7ZBN3; E1P5M0;
E1P607; O14661; O14663; O60517; Q5W084; Q5W086; Q5W087; Q5XKI6;
Q6GMS8; Q9H0Z0; Q9H1T7; Q9H1T8; Q9UIX5;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 3.
22-NOV-2017, entry version 172.
RecName: Full=Syntaxin-16;
Short=Syn16;
Name=STX16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D).
TISSUE=Brain;
PubMed=9587053;
Simonsen A., Bremnes B., Ronning E., Aasland R., Stenmark H.;
"Syntaxin-16, a putative Golgi t-SNARE.";
Eur. J. Cell Biol. 75:223-231(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
PubMed=9464276; DOI=10.1006/bbrc.1997.8029;
Tang B.L., Low D.Y.H., Lee S.S., Tan A.E.H., Ho W.;
"Molecular cloning and localization of human syntaxin 16, a member of
the syntaxin family of SNARE proteins.";
Biochem. Biophys. Res. Commun. 242:673-679(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND E).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-251 (ISOFORM 6).
TISSUE=Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
INVOLVEMENT IN PHP1B.
PubMed=14561710; DOI=10.1172/JCI19159;
Bastepe M., Froehlich L.F., Hendy G.N., Indridason O.S., Josse R.G.,
Koshiyama H., Koerkkoe J., Nakamoto J.M., Rosenbloom A.L.,
Slyper A.H., Sugimoto T., Tsatsoulis A., Crawford J.D., Jueppner H.;
"Autosomal dominant pseudohypoparathyroidism type Ib is associated
with a heterozygous microdeletion that likely disrupts a putative
imprinting control element of GNAS.";
J. Clin. Invest. 112:1255-1263(2003).
[8]
INVOLVEMENT IN PHP1B.
PubMed=15800843; DOI=10.1086/429932;
Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.;
"A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism
type Ib redefines the boundaries of a cis-acting imprinting control
element of GNAS.";
Am. J. Hum. Genet. 76:804-814(2005).
[9]
FUNCTION, AND INTERACTION WITH GCC2.
PubMed=18195106; DOI=10.1083/jcb.200707136;
Ganley I.G., Espinosa E., Pfeffer S.R.;
"A syntaxin 10-SNARE complex distinguishes two distinct transport
routes from endosomes to the trans-Golgi in human cells.";
J. Cell Biol. 180:159-172(2008).
-!- FUNCTION: SNARE involved in vesicular transport from the late
endosomes to the trans-Golgi network.
{ECO:0000269|PubMed:18195106}.
-!- SUBUNIT: Interacts with GCC2. {ECO:0000269|PubMed:18195106}.
-!- INTERACTION:
P50222:MEOX2; NbExp=3; IntAct=EBI-2853548, EBI-748397;
Q9H115:NAPB; NbExp=4; IntAct=EBI-9089968, EBI-3921185;
O95721:SNAP29; NbExp=4; IntAct=EBI-9089968, EBI-490676;
Q12846:STX4; NbExp=3; IntAct=EBI-2853548, EBI-744942;
O75379:VAMP4; NbExp=4; IntAct=EBI-9089968, EBI-744953;
O95183:VAMP5; NbExp=3; IntAct=EBI-2853548, EBI-10191195;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
IV membrane protein.
-!- SUBCELLULAR LOCATION: Isoform C: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=B;
IsoId=O14662-1; Sequence=Displayed;
Name=A;
IsoId=O14662-2; Sequence=VSP_006348;
Name=C;
IsoId=O14662-3; Sequence=VSP_006349, VSP_006350, VSP_006351;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=D;
IsoId=O14662-4; Sequence=VSP_006349;
Name=E;
IsoId=O14662-5; Sequence=VSP_043849;
Name=6;
IsoId=O14662-6; Sequence=VSP_045073;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A
disorder characterized by end-organ resistance to parathyroid
hormone, hypocalcemia and hyperphosphatemia. Patients affected
with PHP1B lack developmental defects characteristic of Albright
hereditary osteodystrophy, and typically show no other endocrine
abnormalities besides resistance to PTH.
{ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15800843}.
Note=The gene represented in this entry is involved in disease
pathogenesis. Microdeletions involving STX16 can cause loss of
methylation at exon A/B of GNAS, resulting in PHP1B.
-!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB69282.1; Type=Frameshift; Positions=142, 163, 165; Evidence={ECO:0000305};
Sequence=AAB69283.1; Type=Frameshift; Positions=142, 163, 165; Evidence={ECO:0000305};
Sequence=AAC05647.1; Type=Frameshift; Positions=142, 163, 165; Evidence={ECO:0000305};
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EMBL; AF008936; AAB69283.1; ALT_FRAME; mRNA.
EMBL; AF008935; AAB69282.1; ALT_FRAME; mRNA.
EMBL; AF008937; AAB69284.1; -; mRNA.
EMBL; AF038897; AAC05647.1; ALT_FRAME; mRNA.
EMBL; AL139349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL050327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75481.1; -; Genomic_DNA.
EMBL; CH471077; EAW75482.1; -; Genomic_DNA.
EMBL; CH471077; EAW75484.1; -; Genomic_DNA.
EMBL; CH471077; EAW75485.1; -; Genomic_DNA.
EMBL; CH471077; EAW75486.1; -; Genomic_DNA.
EMBL; BC019042; AAH19042.1; -; mRNA.
EMBL; BC073876; AAH73876.1; -; mRNA.
EMBL; BX396221; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS13468.1; -. [O14662-1]
CCDS; CCDS13469.1; -. [O14662-2]
CCDS; CCDS46619.1; -. [O14662-5]
CCDS; CCDS46620.1; -. [O14662-4]
CCDS; CCDS56199.1; -. [O14662-6]
PIR; JC5927; JC5927.
RefSeq; NP_001001433.1; NM_001001433.2. [O14662-1]
RefSeq; NP_001128244.1; NM_001134772.2. [O14662-5]
RefSeq; NP_001128245.1; NM_001134773.2. [O14662-4]
RefSeq; NP_001191797.1; NM_001204868.1. [O14662-6]
RefSeq; NP_003754.2; NM_003763.5. [O14662-2]
UniGene; Hs.307913; -.
ProteinModelPortal; O14662; -.
SMR; O14662; -.
BioGrid; 114223; 18.
CORUM; O14662; -.
DIP; DIP-57570N; -.
IntAct; O14662; 14.
MINT; MINT-1196639; -.
STRING; 9606.ENSP00000360183; -.
iPTMnet; O14662; -.
PhosphoSitePlus; O14662; -.
BioMuta; STX16; -.
EPD; O14662; -.
MaxQB; O14662; -.
PaxDb; O14662; -.
PeptideAtlas; O14662; -.
PRIDE; O14662; -.
DNASU; 8675; -.
Ensembl; ENST00000355957; ENSP00000348229; ENSG00000124222. [O14662-4]
Ensembl; ENST00000358029; ENSP00000350723; ENSG00000124222. [O14662-5]
Ensembl; ENST00000359617; ENSP00000352634; ENSG00000124222. [O14662-6]
Ensembl; ENST00000361830; ENSP00000354445; ENSG00000124222. [O14662-6]
Ensembl; ENST00000371132; ENSP00000360173; ENSG00000124222. [O14662-2]
Ensembl; ENST00000371141; ENSP00000360183; ENSG00000124222. [O14662-1]
Ensembl; ENST00000467096; ENSP00000434369; ENSG00000124222. [O14662-3]
GeneID; 8675; -.
KEGG; hsa:8675; -.
UCSC; uc002xzi.4; human. [O14662-1]
CTD; 8675; -.
DisGeNET; 8675; -.
EuPathDB; HostDB:ENSG00000124222.21; -.
GeneCards; STX16; -.
HGNC; HGNC:11431; STX16.
HPA; HPA041019; -.
HPA; HPA042033; -.
MalaCards; STX16; -.
MIM; 603233; phenotype.
MIM; 603666; gene.
neXtProt; NX_O14662; -.
OpenTargets; ENSG00000124222; -.
Orphanet; 94089; Pseudohypoparathyroidism type 1B.
PharmGKB; PA36231; -.
eggNOG; KOG0809; Eukaryota.
eggNOG; COG5325; LUCA.
GeneTree; ENSGT00880000138049; -.
HOGENOM; HOG000190358; -.
HOVERGEN; HBG057612; -.
InParanoid; O14662; -.
KO; K08489; -.
OMA; RENQSSC; -.
OrthoDB; EOG091G0GY1; -.
PhylomeDB; O14662; -.
TreeFam; TF314090; -.
Reactome; R-HSA-6811438; Intra-Golgi traffic.
Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
SIGNOR; O14662; -.
ChiTaRS; STX16; human.
GeneWiki; STX16; -.
GenomeRNAi; 8675; -.
PRO; PR:O14662; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124222; -.
ExpressionAtlas; O14662; baseline and differential.
Genevisible; O14662; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0031201; C:SNARE complex; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC.
GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
InterPro; IPR010989; SNARE.
InterPro; IPR028673; STX16.
InterPro; IPR006012; Syntaxin/epimorphin_CS.
InterPro; IPR006011; Syntaxin_N.
InterPro; IPR000727; T_SNARE_dom.
PANTHER; PTHR19957:SF141; PTHR19957:SF141; 1.
Pfam; PF05739; SNARE; 1.
Pfam; PF00804; Syntaxin; 1.
SMART; SM00397; t_SNARE; 1.
SUPFAM; SSF47661; SSF47661; 1.
PROSITE; PS00914; SYNTAXIN; 1.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 325 Syntaxin-16.
/FTId=PRO_0000210226.
TOPO_DOM 1 301 Cytoplasmic. {ECO:0000255}.
TRANSMEM 302 322 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 323 325 Vesicular. {ECO:0000255}.
DOMAIN 230 292 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BVI5}.
VAR_SEQ 1 53 Missing (in isoform 6).
{ECO:0000303|Ref.6}.
/FTId=VSP_045073.
VAR_SEQ 28 48 Missing (in isoform A).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9587053}.
/FTId=VSP_006348.
VAR_SEQ 28 44 Missing (in isoform C and isoform D).
{ECO:0000303|PubMed:9464276,
ECO:0000303|PubMed:9587053}.
/FTId=VSP_006349.
VAR_SEQ 45 48 Missing (in isoform E).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043849.
VAR_SEQ 132 132 L -> A (in isoform C).
{ECO:0000303|PubMed:9587053}.
/FTId=VSP_006350.
VAR_SEQ 133 325 Missing (in isoform C).
{ECO:0000303|PubMed:9587053}.
/FTId=VSP_006351.
CONFLICT 99 99 L -> S (in Ref. 1; AAB69282/AAB69283).
{ECO:0000305}.
CONFLICT 147 147 A -> E (in Ref. 1; AAC05647).
{ECO:0000305}.
CONFLICT 243 243 I -> M (in Ref. 1; AAB69282/AAB69283).
{ECO:0000305}.
SEQUENCE 325 AA; 37031 MW; 65F566541A042C3C CRC64;
MATRRLTDAF LLLRNNSIQN RQLLAEQVSS HITSSPLHSR SIAAELDELA DDRMALVSGI
SLDPEAAIGV TKRPPPKWVD GVDEIQYDVG RIKQKMKELA SLHDKHLNRP TLDDSSEEEH
AIEITTQEIT QLFHRCQRAV QALPSRARAC SEQEGRLLGN VVASLAQALQ ELSTSFRHAQ
SGYLKRMKNR EERSQHFFDT SVPLMDDGDD NTLYHRGFTE DQLVLVEQNT LMVEEREREI
RQIVQSISDL NEIFRDLGAM IVEQGTVLDR IDYNVEQSCI KTEDGLKQLH KAEQYQKKNR
KMLVILILFV IIIVLIVVLV GVKSR


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