ID   STAP2_MOUSE             Reviewed;         411 AA.
AC   Q8R0L1; Q8BWS2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Signal-transducing adaptor protein 2;
DE            Short=STAP-2;
GN   Name=Stap2;
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 [MRNA] (ISOFORM 1), INTERACTION WITH CSF1R, FUNCTION,
RP   TISSUE SPECIFICITY, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Fetal liver;
RX   PubMed=12540842; DOI=10.1074/jbc.m211230200;
RA   Minoguchi M., Minoguchi S., Aki D., Joo A., Yamamoto T., Yumioka T.,
RA   Matsuda T., Yoshimura A.;
RT   "STAP-2/BKS, an adaptor/docking protein, modulates STAT3 activation in
RT   acute-phase response through its YXXQ motif.";
RL   J. Biol. Chem. 278:11182-11189(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
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: Substrate of protein kinase PTK6 (By similarity). May play a
CC       regulatory role in the acute-phase response in systemic inflammation
CC       and may modulate STAT3 activity. {ECO:0000250,
CC       ECO:0000269|PubMed:12540842}.
CC   -!- SUBUNIT: Interacts with PTK6 and CSF1R. {ECO:0000269|PubMed:12540842}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12540842}. Membrane
CC       {ECO:0000269|PubMed:12540842}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12540842}. Note=The translocation to the membranes
CC       occurs in response to EGF when the protein is overexpressed in
CC       fibroblastic cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R0L1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R0L1-2; Sequence=VSP_013401, VSP_013402;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12540842}.
CC   -!- PTM: Phosphorylated on tyrosine. Phosphorylated by PTK6 at Tyr-250
CC       modulates PTK6-mediated STAT3 activation. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK050131; BAC34083.1; -; mRNA.
DR   EMBL; AK050172; BAC34107.1; -; mRNA.
DR   EMBL; BC026642; AAH26642.1; -; mRNA.
DR   CCDS; CCDS28889.1; -. [Q8R0L1-1]
DR   RefSeq; NP_666046.1; NM_145934.2. [Q8R0L1-1]
DR   RefSeq; XP_017172690.1; XM_017317201.1.
DR   AlphaFoldDB; Q8R0L1; -.
DR   SMR; Q8R0L1; -.
DR   BioGRID; 223125; 6.
DR   STRING; 10090.ENSMUSP00000038130; -.
DR   iPTMnet; Q8R0L1; -.
DR   PhosphoSitePlus; Q8R0L1; -.
DR   MaxQB; Q8R0L1; -.
DR   PaxDb; 10090-ENSMUSP00000038130; -.
DR   PeptideAtlas; Q8R0L1; -.
DR   ProteomicsDB; 258638; -. [Q8R0L1-1]
DR   ProteomicsDB; 258639; -. [Q8R0L1-2]
DR   Antibodypedia; 1197; 337 antibodies from 35 providers.
DR   DNASU; 106766; -.
DR   Ensembl; ENSMUST00000043785.8; ENSMUSP00000038130.7; ENSMUSG00000038781.8. [Q8R0L1-1]
DR   GeneID; 106766; -.
DR   KEGG; mmu:106766; -.
DR   UCSC; uc008dao.3; mouse. [Q8R0L1-1]
DR   AGR; MGI:2147039; -.
DR   CTD; 55620; -.
DR   MGI; MGI:2147039; Stap2.
DR   VEuPathDB; HostDB:ENSMUSG00000038781; -.
DR   eggNOG; ENOG502QURW; Eukaryota.
DR   GeneTree; ENSGT00530000063841; -.
DR   HOGENOM; CLU_043957_0_0_1; -.
DR   InParanoid; Q8R0L1; -.
DR   OMA; SQLPPCY; -.
DR   OrthoDB; 4259410at2759; -.
DR   PhylomeDB; Q8R0L1; -.
DR   TreeFam; TF332087; -.
DR   Reactome; R-MMU-8849474; PTK6 Activates STAT3.
DR   BioGRID-ORCS; 106766; 1 hit in 76 CRISPR screens.
DR   PRO; PR:Q8R0L1; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8R0L1; Protein.
DR   Bgee; ENSMUSG00000038781; Expressed in intestinal villus and 239 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR   CDD; cd10404; SH2_STAP2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR039111; STAP1/STAP2.
DR   InterPro; IPR035878; STAP2_SH2.
DR   PANTHER; PTHR16186:SF11; SIGNAL-TRANSDUCING ADAPTOR PROTEIN 2; 1.
DR   PANTHER; PTHR16186; SIGNAL-TRANSDUCING ADAPTOR PROTEIN-RELATED; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   Genevisible; Q8R0L1; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW   Reference proteome; SH2 domain.
FT   CHAIN           1..411
FT                   /note="Signal-transducing adaptor protein 2"
FT                   /id="PRO_0000072240"
FT   DOMAIN          20..120
FT                   /note="PH"
FT   DOMAIN          152..248
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          291..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          390..410
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        349..363
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT   MOD_RES         250
FT                   /note="Phosphotyrosine; by PTK6"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT   MOD_RES         318
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT   MOD_RES         330
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGK3"
FT   VAR_SEQ         256..272
FT                   /note="FVDSDRENGESAWAVPS -> VCDVGLPGLDRDTLSGG (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013401"
FT   VAR_SEQ         273..411
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013402"
SQ   SEQUENCE   411 AA;  45802 MW;  485C00B703C470A8 CRC64;
     MATALSPPRG PKLKGAPPSH YYESFLEKKG PCDQDYRKFW AGLQGLAICF YNSNRDLQPL
     EKLDLRLFSK LRDEALLGSS RDTAYHFSLV LRDQEVKFKV ESLESCEMWK GFILTVVELR
     VPSNLTLLPG HLYMMAEVLT KEEVRRAAEV PWCFLQVSRL EAQLLLERYP ECGNLLLRPG
     GDGKDSVSVT TRQILNGSPV VKHYKVKRAG SKYVIDVEDP FSCPSLEAVV NYFVTHTKRA
     LVPFLLDEDY EKVLGFVDSD RENGESAWAV PSFRASGPAL PANVLKPLPP VPVSVSSQED
     KLPQLPPLPQ LPDTDENYVT PIEDSPAAEY MNQDVSLSSQ AVPLKPKKPA RLPAKPPKPS
     VVPKPDLKAI TSVWTRKLGG SSSQASSLVT RLGDITAELE EKLQKRRALE H
//