SH319_MOUSE
ID SH319_MOUSE Reviewed; 789 AA.
AC Q91X43; O08635; O35146; Q8C7I2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=SH3 domain-containing protein 19;
DE AltName: Full=Kryn;
GN Name=Sh3d19;
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 2), TISSUE SPECIFICITY, AND INTERACTION
RP WITH SH3YL1.
RX PubMed=12615363; DOI=10.1016/s0923-1811(02)00140-8;
RA Shimomura Y., Aoki N., Ito K., Ito M.;
RT "Gene expression of Sh3d19, a novel adaptor protein with five Src homology
RT 3 domains, in anagen mouse hair follicles.";
RL J. Dermatol. Sci. 31:43-51(2003).
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 13-789 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, and Kidney;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 465-789.
RA Sekely S.A., Kay B.K.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 505-789.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: May play a role in regulating A disintegrin and
CC metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May
CC be involved in suppression of Ras-induced cellular transformation and
CC Ras-mediated activation of ELK1. Plays a role in the regulation of cell
CC morphology and cytoskeletal organization (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ADAM12. Isoform 2 (but not isoform 1) interacts
CC with ADAM9, ADAM10, ADAM15 and ADAM17. Interacts with SH3GL1 SH3
CC domain. Interacts via SH3 3 and SH3 4 or SH3 4 and SH3 5 domains with
CC SOS2. Probably forms a trimeric complex with SH3GL1 and SOS2 (By
CC similarity). Interacts with SH3YL1. {ECO:0000250,
CC ECO:0000269|PubMed:12615363}.
CC -!- INTERACTION:
CC Q91X43; O08641: Sh3yl1; NbExp=3; IntAct=EBI-2024543, EBI-2024519;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91X43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91X43-2; Sequence=VSP_031185;
CC -!- TISSUE SPECIFICITY: Expressed in hair follicles.
CC {ECO:0000269|PubMed:12615363}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB82091.1; Type=Miscellaneous discrepancy; Note=Sequence contamination. Potential vector sequence.; Evidence={ECO:0000305};
CC Sequence=AAH12633.1; Type=Miscellaneous discrepancy; Note=Sequence contamination. Potential vector sequence.; Evidence={ECO:0000305};
CC Sequence=AAH31117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; D89677; BAA19686.2; -; mRNA.
DR EMBL; AC133508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012633; AAH12633.1; ALT_SEQ; mRNA.
DR EMBL; BC031117; AAH31117.1; ALT_INIT; mRNA.
DR EMBL; AF003234; AAB82091.1; ALT_SEQ; mRNA.
DR EMBL; AK050185; BAC34114.1; -; mRNA.
DR RefSeq; NP_001075883.2; NM_001082414.2.
DR AlphaFoldDB; Q91X43; -.
DR SMR; Q91X43; -.
DR BioGRID; 205114; 5.
DR IntAct; Q91X43; 2.
DR STRING; 10090.ENSMUSP00000138320; -.
DR iPTMnet; Q91X43; -.
DR PhosphoSitePlus; Q91X43; -.
DR jPOST; Q91X43; -.
DR MaxQB; Q91X43; -.
DR PaxDb; Q91X43; -.
DR PeptideAtlas; Q91X43; -.
DR PRIDE; Q91X43; -.
DR ProteomicsDB; 255402; -. [Q91X43-1]
DR ProteomicsDB; 255403; -. [Q91X43-2]
DR Antibodypedia; 2969; 105 antibodies from 20 providers.
DR Ensembl; ENSMUST00000107664; ENSMUSP00000103291; ENSMUSG00000028082. [Q91X43-1]
DR Ensembl; ENSMUST00000182666; ENSMUSP00000138320; ENSMUSG00000028082. [Q91X43-1]
DR Ensembl; ENSMUST00000238222; ENSMUSP00000158775; ENSMUSG00000028082. [Q91X43-1]
DR Ensembl; ENSMUST00000238331; ENSMUSP00000158600; ENSMUSG00000028082. [Q91X43-1]
DR GeneID; 27059; -.
DR KEGG; mmu:27059; -.
DR UCSC; uc008pra.2; mouse. [Q91X43-1]
DR CTD; 152503; -.
DR MGI; MGI:1350923; Sh3d19.
DR VEuPathDB; HostDB:ENSMUSG00000028082; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000155694; -.
DR HOGENOM; CLU_015305_2_0_1; -.
DR InParanoid; Q91X43; -.
DR OMA; VHKSCMK; -.
DR OrthoDB; 288421at2759; -.
DR PhylomeDB; Q91X43; -.
DR TreeFam; TF330850; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 27059; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Sh3d19; mouse.
DR PRO; PR:Q91X43; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91X43; protein.
DR Bgee; ENSMUSG00000028082; Expressed in choroid plexus epithelium and 256 other tissues.
DR ExpressionAtlas; Q91X43; baseline and differential.
DR Genevisible; Q91X43; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR CDD; cd11814; SH3_Eve1_1; 1.
DR CDD; cd11816; SH3_Eve1_3; 1.
DR InterPro; IPR035834; Eve1_SH3_1.
DR InterPro; IPR035835; Eve1_SH3_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF50044; SSF50044; 5.
DR PROSITE; PS50002; SH3; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..789
FT /note="SH3 domain-containing protein 19"
FT /id="PRO_0000318198"
FT DOMAIN 414..476
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 494..553
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 570..629
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 660..719
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 729..788
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 24..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..369
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12615363"
FT /id="VSP_031185"
FT CONFLICT 559
FT /note="S -> G (in Ref. 5; BAC34114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 86077 MW; D3F866FB1A5BEB81 CRC64;
MNIMNTEQSQ NTIVSRIKAF EGQTNTEIPG LPKKPEIIPR TIPPKPAVSS GKPLVAPKPA
ANRASGEWDT WAENRLKVTS REGLTPYSSP QEAGITPVTK PELPKKPTPG LTRSVNHETS
GGRPMAESPD TGKKIPTPAP RPLLPKKSAS TDAPPYPSIP PKLVSAPPRL SVASQAKAFR
SLGEGLPSNP PVPAPQSKAL GDIDLISFDD DVLPTSGSPA EEPTGSETVL DPFQLPTKTE
ATKERAVQPA PTRKPTVIRI PAKPGKCLHE EPQSPPPLPA EKPVGNTHSA VSGRPSHSDR
TRNPELEQAS ESGGLVQGPP RLPPRPVHGK VIPVWRPPPK GAPERPPPPK LPASKSSNKN
LPFNRSSSDM DLQKKQSHFV SGLSKAKSQI FKNQDPVLPP RPKPGHPLYR KYMLSVPHGI
ANEDIVSRNP TELSCKRGDV LVILKQAENN YLECQRGEGT GRVHPSQMKI VTPLDERPRG
RPNDSGHSQK PVDSGAPHAV ALHDFPAEQA DDLSLTSGEI VYLLEKIDAE WYRGKCRNQT
GVFPANYVKV IVDIPEGRSG KRESFSSHCA KGPRCVARFE YIGDQKDELS FSEGEVIILT
EYVNEEWGRG EIRDRSGIFP LNFVELVGDH PTSGANILST KVPPKTKNED PGSNSQDSSP
PGEWCKALHS FTAETSEDLP FKRGDRILIL ERLDSDWYRG RLHDREGIFP AVFVQPCPAE
AKGVASAIPK GRKVKALYDF LGENEDELSF KAGDVITELE PIDDAWMRGE LMGRAGMFPK
NYVQFLQVS
