SPT13_MOUSE
ID SPT13_MOUSE Reviewed; 656 AA.
AC Q5DU57; Q3TZ09;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Spermatogenesis-associated protein 13;
DE AltName: Full=APC-stimulated guanine nucleotide exchange factor 2;
DE Short=Asef2;
GN Name=Spata13;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-656 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19893577; DOI=10.1038/embor.2009.233;
RA Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
RA Ohwada S., Akiyama T.;
RT "The adenomatous polyposis coli-associated exchange factors Asef and Asef2
RT are required for adenoma formation in Apc(Min/+)mice.";
RL EMBO Rep. 10:1355-1362(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
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: Acts as guanine nucleotide exchange factor (GEF) for RHOA,
CC RAC1 and CDC42 GTPases. Regulates cell migration and adhesion assembly
CC and disassembly through a RAC1, PI3K, RHOA and AKT1-dependent
CC mechanism. Increases both RAC1 and CDC42 activity, but decreases the
CC amount of active RHOA (By similarity). Required for MMP9 up-regulation
CC via the JNK signaling pathway in colorectal tumor cells. Involved in
CC tumor angiogenesis and may play a role in intestinal adenoma formation
CC and tumor progression. {ECO:0000250, ECO:0000269|PubMed:19893577}.
CC -!- ACTIVITY REGULATION: Both the ABR and the SH3 domains contribute to
CC maintaining the protein in an inhibited conformation by associating
CC with the C-terminal tail. Binding of these domains to the C-terminal
CC tail inhibits the activity of the protein by blocking a region that is
CC required for its GEF activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via ABR and SH3 domain) with APC. The binding of
CC APC enhances its GEF activity by relieving it from an autoinhibitory
CC conformation, in which the ABR and SH3 domains are associated with the
CC C-terminal tail. Interacts (via C-terminal tail) with PPP1R9B (via C-
CC terminus). Interacts with RAC1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC filopodium {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}.
CC Cell projection, ruffle membrane {ECO:0000250}. Note=Accumulates in the
CC lamellipodium and ruffle membrane in response to hepatocyte growth
CC factor (HGF) treatment. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5DU57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DU57-2; Sequence=VSP_023287;
CC -!- TISSUE SPECIFICITY: Expression is aberrantly enhanced in most
CC colorectal tumors. {ECO:0000269|PubMed:19893577}.
CC -!- DOMAIN: The C-terminal tail is required for its GEF activity.
CC {ECO:0000250}.
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DR EMBL; AK158193; BAE34401.1; -; mRNA.
DR EMBL; AC151835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220313; BAD90389.1; -; mRNA.
DR RefSeq; NP_001028444.1; NM_001033272.2.
DR RefSeq; NP_001297523.1; NM_001310594.1.
DR AlphaFoldDB; Q5DU57; -.
DR SMR; Q5DU57; -.
DR BioGRID; 230117; 2.
DR IntAct; Q5DU57; 2.
DR STRING; 10090.ENSMUSP00000022566; -.
DR iPTMnet; Q5DU57; -.
DR PhosphoSitePlus; Q5DU57; -.
DR EPD; Q5DU57; -.
DR MaxQB; Q5DU57; -.
DR PaxDb; Q5DU57; -.
DR PeptideAtlas; Q5DU57; -.
DR PRIDE; Q5DU57; -.
DR ProteomicsDB; 254542; -. [Q5DU57-1]
DR ProteomicsDB; 254543; -. [Q5DU57-2]
DR GeneID; 219140; -.
DR KEGG; mmu:219140; -.
DR UCSC; uc007ufe.2; mouse. [Q5DU57-1]
DR CTD; 221178; -.
DR MGI; MGI:104838; Spata13.
DR eggNOG; KOG3519; Eukaryota.
DR InParanoid; Q5DU57; -.
DR OrthoDB; 507598at2759; -.
DR PhylomeDB; Q5DU57; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 219140; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Spata13; mouse.
DR PRO; PR:Q5DU57; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5DU57; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..656
FT /note="Spermatogenesis-associated protein 13"
FT /id="PRO_0000278449"
FT DOMAIN 151..210
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 244..428
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 459..565
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..154
FT /note="ABR (APC-binding region) domain"
FT /evidence="ECO:0000250"
FT REGION 215..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..656
FT /note="C-terminal tail"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..352
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023287"
SQ SEQUENCE 656 AA; 75257 MW; B85BB725EC3059E2 CRC64;
MHPASVTTTS QDPCAPSGSC RGGRRRRPIS VIGGVSFYGN TQVEDVENLL VQPAARPPVP
AHQVPPYKAV SARLRPFTFS QSTPIGLDRV GRRRQMKTSN VSSDGGAESS ALVDDNGSEE
DFSYEELCQA NPRYLQPGGE QLAINELISD GSVVCAEALW DHVTMDDQEL GFKAGDVIQV
LEASNKDWWW GRNEDKEAWF PASFVRLRVN QEELPENCSS SHGEEQDEDT SKARHKHPES
QQQMRTNVIQ EIMNTERVYI KHLKDICEGY IRQCRKHTGM FTVAQLATIF GNIEDIYKFQ
RKFLKDLEKQ YNKEEPHLSE IGSCFLEHQE GFAIYSEYCN NHPGACVELS NLMKHSKYRH
FFEACRLLQQ MIDIALDGFL LTPVQKICKY PLQLAELLKY TTQEHGDYNN IKAAYEAMKN
VACLINERKR KLESIDKIAR WQVSIVGWEG LDILDRSSEL IHSGELTKIT RQGKSQQRIF
FLFDHQLVSC KKDLLRRDML YYKGRMDMDE VELVDVEDGR DKDWSLSLRN AFKLVSKATD
EVHLFCARKQ EDKARWLQAY ADERRRVQED QQMGMEIPEN QKKLAMLNAQ KAGHGKSKGY
NSCPVAPPHQ SLPPLHQRHI TVPTSIPQQQ VFALAEPKRK PSIFWHTFHK LTPFRK
