SDCB2_MOUSE
ID SDCB2_MOUSE Reviewed; 292 AA.
AC Q99JZ0; Q3UN51;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Syntenin-2;
DE AltName: Full=Syndecan-binding protein 2;
GN Name=Sdcbp2;
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 MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cecum {ECO:0000312|EMBL:BAE23054.1},
RC Gall bladder {ECO:0000312|EMBL:BAE25896.1}, and
RC Stomach {ECO:0000312|EMBL:BAE35814.1};
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 [2]
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).
CC -!- FUNCTION: Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play
CC a role in the organization of nuclear PIP2, cell division and cell
CC survival. {ECO:0000250|UniProtKB:Q9H190}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with SDCBP. Interacts with
CC TM4SF1. {ECO:0000250|UniProtKB:Q9H190}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H190}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H190}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9H190}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H190}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9H190}. Note=Associates with intracellular
CC membranes and enriched in the apical region of the cell and in
CC intracellular compartments. Colocalizes with TM4SF1 in the apical
CC region of the cell. Predominantly targeted to nuclear PIP2 pools.
CC Shuttles between several subcellular compartments. PIP2 plays an
CC important role in the distribution of SDCBP2.
CC {ECO:0000250|UniProtKB:Q9H190}.
CC -!- DOMAIN: The two PDZ domains mediate the interaction with
CC phosphatidylinositol 4,5-bisphosphate (PIP2) and target SDCBP2 to the
CC plasma membranes and nucleoli, PIP2-rich regions.
CC {ECO:0000250|UniProtKB:Q9H190}.
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DR EMBL; AK136572; BAE23054.1; -; mRNA.
DR EMBL; AK144452; BAE25896.1; -; mRNA.
DR EMBL; AK160483; BAE35814.1; -; mRNA.
DR EMBL; BC005556; AAH05556.1; -; mRNA.
DR CCDS; CCDS16870.1; -.
DR RefSeq; NP_663510.1; NM_145535.2.
DR RefSeq; XP_006499367.1; XM_006499304.2.
DR RefSeq; XP_006499368.1; XM_006499305.1.
DR AlphaFoldDB; Q99JZ0; -.
DR SMR; Q99JZ0; -.
DR MINT; Q99JZ0; -.
DR STRING; 10090.ENSMUSP00000028950; -.
DR PhosphoSitePlus; Q99JZ0; -.
DR MaxQB; Q99JZ0; -.
DR PaxDb; Q99JZ0; -.
DR PRIDE; Q99JZ0; -.
DR ProteomicsDB; 256758; -.
DR Antibodypedia; 23059; 244 antibodies from 30 providers.
DR DNASU; 228765; -.
DR Ensembl; ENSMUST00000028950; ENSMUSP00000028950; ENSMUSG00000027456.
DR GeneID; 228765; -.
DR KEGG; mmu:228765; -.
DR UCSC; uc008nec.2; mouse.
DR CTD; 27111; -.
DR MGI; MGI:2385156; Sdcbp2.
DR VEuPathDB; HostDB:ENSMUSG00000027456; -.
DR eggNOG; ENOG502S0HE; Eukaryota.
DR GeneTree; ENSGT00940000161179; -.
DR HOGENOM; CLU_059870_0_0_1; -.
DR InParanoid; Q99JZ0; -.
DR OMA; AVCEVNG; -.
DR OrthoDB; 1035679at2759; -.
DR PhylomeDB; Q99JZ0; -.
DR TreeFam; TF327131; -.
DR BioGRID-ORCS; 228765; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Trappc4; mouse.
DR PRO; PR:Q99JZ0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99JZ0; protein.
DR Bgee; ENSMUSG00000027456; Expressed in right colon and 114 other tissues.
DR Genevisible; Q99JZ0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Lipid-binding; Membrane; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..292
FT /note="Syntenin-2"
FT /id="PRO_0000184005"
FT DOMAIN 108..187
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 192..267
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
SQ SEQUENCE 292 AA; 31565 MW; C694316BC0A0931D CRC64;
MSVLYPSLED LKVGQVIQAQ GRASPTMPTL PAPMASAPPL SELYPNLAEL ESYMGLSLSS
QEVQKNLTQI PDSDNMVVTS PGPGQVVAPV SGNNLGILRA EIKPGVREIH LCKDERGKTG
LRLQAVDKGL FVQLVQANTP ASLVGLRFGD QILQIDGCDC AGWNTHKAHK VLKKASAEKI
VMVIRDRPFQ RTVTMHKDSS GQVGFSIKKG KIVSVVKGSS AARNGLLTNH YVCEVNGQNV
IGLKDKKVTE ILTTAGDVIT LTIIPTVIYE HMIKRLSPLL LHHTMDHSIP DT
