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   27-MAR-2024, entry version 136.
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};
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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.ENSMUSP00000158775; -.
DR   iPTMnet; Q91X43; -.
DR   PhosphoSitePlus; Q91X43; -.
DR   jPOST; Q91X43; -.
DR   MaxQB; Q91X43; -.
DR   PaxDb; 10090-ENSMUSP00000138320; -.
DR   PeptideAtlas; Q91X43; -.
DR   ProteomicsDB; 255402; -. [Q91X43-1]
DR   ProteomicsDB; 255403; -. [Q91X43-2]
DR   Pumba; Q91X43; -.
DR   Antibodypedia; 2969; 122 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000107664.3; ENSMUSP00000103291.3; ENSMUSG00000028082.15. [Q91X43-1]
DR   Ensembl; ENSMUST00000182666.8; ENSMUSP00000138320.2; ENSMUSG00000028082.15. [Q91X43-1]
DR   Ensembl; ENSMUST00000238222.2; ENSMUSP00000158775.2; ENSMUSG00000028082.15. [Q91X43-1]
DR   Ensembl; ENSMUST00000238331.2; ENSMUSP00000158600.2; ENSMUSG00000028082.15. [Q91X43-1]
DR   GeneID; 27059; -.
DR   KEGG; mmu:27059; -.
DR   UCSC; uc008pra.2; mouse. [Q91X43-1]
DR   AGR; MGI:1350923; -.
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; 2920126at2759; -.
DR   PhylomeDB; Q91X43; -.
DR   TreeFam; TF330850; -.
DR   Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR   BioGRID-ORCS; 27059; 3 hits in 76 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 259 other cell types or tissues.
DR   ExpressionAtlas; Q91X43; baseline and differential.
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   Gene3D; 2.30.30.40; SH3 Domains; 4.
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   PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR   Pfam; PF00018; SH3_1; 3.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 5.
DR   SUPFAM; SSF50044; SH3-domain; 5.
DR   PROSITE; PS50002; SH3; 5.
DR   Genevisible; Q91X43; MM.
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
//