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Database: UniProt
Entry: D3ZYM5_RAT
LinkDB: D3ZYM5_RAT
Original site: D3ZYM5_RAT 
ID   D3ZYM5_RAT              Unreviewed;       790 AA.
AC   D3ZYM5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=MTSS I-BAR domain containing 1 {ECO:0000313|Ensembl:ENSRNOP00000011984.4};
GN   Name=Mtss1 {ECO:0000313|Ensembl:ENSRNOP00000011984.4,
GN   ECO:0000313|RGD:1309883};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000011984.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000011984.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000011984.4,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000011984.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000011984.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; NP_001124035.1; NM_001130563.1.
DR   AlphaFoldDB; D3ZYM5; -.
DR   SMR; D3ZYM5; -.
DR   STRING; 10116.ENSRNOP00000011984; -.
DR   PhosphoSitePlus; D3ZYM5; -.
DR   PaxDb; 10116-ENSRNOP00000011984; -.
DR   Ensembl; ENSRNOT00000011984.6; ENSRNOP00000011984.4; ENSRNOG00000009001.7.
DR   GeneID; 362918; -.
DR   KEGG; rno:362918; -.
DR   AGR; RGD:1309883; -.
DR   CTD; 9788; -.
DR   RGD; 1309883; Mtss1.
DR   eggNOG; ENOG502QRG4; Eukaryota.
DR   GeneTree; ENSGT00950000183156; -.
DR   OMA; AGAFPHC; -.
DR   OrthoDB; 3875239at2759; -.
DR   TreeFam; TF320619; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000009001; Expressed in liver and 19 other cell types or tissues.
DR   ExpressionAtlas; D3ZYM5; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR   GO; GO:0005912; C:adherens junction; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0003779; F:actin binding; ISO:RGD.
DR   GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR   GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR   GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR   GO; GO:0030041; P:actin filament polymerization; ISO:RGD.
DR   GO; GO:0034334; P:adherens junction maintenance; ISO:RGD.
DR   GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; ISS:UniProtKB.
DR   GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; ISS:UniProtKB.
DR   GO; GO:0072102; P:glomerulus morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0010960; P:magnesium ion homeostasis; ISO:RGD.
DR   GO; GO:0072170; P:metanephric tubule development; ISO:RGD.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0072160; P:nephron tubule epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR   GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:RGD.
DR   GO; GO:0061333; P:renal tubule morphogenesis; ISS:UniProtKB.
DR   CDD; cd07643; I-BAR_IMD_MIM; 1.
DR   CDD; cd22060; WH2_MTSS1; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR013606; I-BAR_dom.
DR   InterPro; IPR030127; MTSS1/MTSS2.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR15708; ACTIN BUNDLING/MISSING IN METASTASIS-RELATED; 1.
DR   PANTHER; PTHR15708:SF10; PROTEIN MTSS 1; 1.
DR   Pfam; PF08397; IMD; 1.
DR   Pfam; PF02205; WH2; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   PROSITE; PS51338; IMD; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   1: Evidence at protein level;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ   SEQUENCE   790 AA;  85768 MW;  9F7A7AE120CFA840 CRC64;
     MGFAVSVMGT PRPRAQCSRP ESVSCPRRAG KMEAVIEKEC SALGGLFQTI ISDMKGSYPV
     WEDFINKAGK LQSQLRTTVV AAAAFLDAFQ KVADMATNTR GGTREIGSAL TRMCMRHRSI
     EAKLRQFSSA LIDCLINPLQ EQMEEWKKVA NQLDKDHAKE YKKARQEIKK KSSDTLKLQK
     KAKKVDAQGR GDIQPQLDSA LQDVNDKYLL LEETEKQAVR KALIEERGRF CTFISMLRPV
     IEEEISMLGE ITHLQTISED LKSLTMDPHK LPSSSEQVIL DLKGSDYSWS YQTPPSSPST
     TMSRKSSVCS SLNSVNSSDS RSSGSHSHSP SSHYRYRSSN LAQQAPVRLS SVSSHDSGFI
     SQDAFQSKSP SPMPPEAANQ LSNGFSHYSL SSESHAGPVG AGPFPHCLPA SRLLPRVTSI
     HLPDYAHYYT IGPGMFPSSQ IPSWKDWAKP GPYDQPLVNT LQRRKEKREA DSSGGGPTAT
     AGPPAAAEEA QRPRSMTVSA APRPGEDMEA CDELALALSR GLQLDAQRSS RDSLQCSSGY
     STQTTTPCCS EDTIPSQVSD YDYFSVSGDQ EAEQQEFDKS STIPRNSDIS QSYRRMFQAK
     RPASTAGLPT TLGPAMVTPG VATIRRTPST KPSVRRGTIG AGPIPIKTPV IPVKTPTVPD
     LPGVLPSPPD GPEERGEHSP ESPSVGEGPQ GVSNIPSSLW SGHAPINPPL PGPKPSIPEE
     HRQAIPESEA EDQERDPSST SVSPGPIPES DPADLSPRES PQGEDMLNAI RRGVKLKKTT
     TNDRSAPRFS
//
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