GenomeNet

Database: UniProt
Entry: M0RB44_RAT
LinkDB: M0RB44_RAT
Original site: M0RB44_RAT 
ID   M0RB44_RAT              Unreviewed;       857 AA.
AC   M0RB44;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Shroom family member 1 {ECO:0000313|Ensembl:ENSRNOP00000066767.3};
GN   Name=Shroom1 {ECO:0000313|Ensembl:ENSRNOP00000066767.3,
GN   ECO:0000313|RGD:1308066};
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:ENSRNOP00000066767.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000066767.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000066767.3,
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:ENSRNOP00000066767.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000066767.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the shroom family.
CC       {ECO:0000256|ARBA:ARBA00006469}.
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DR   AlphaFoldDB; M0RB44; -.
DR   STRING; 10116.ENSRNOP00000066767; -.
DR   PaxDb; 10116-ENSRNOP00000066767; -.
DR   Ensembl; ENSRNOT00000074769.4; ENSRNOP00000066767.3; ENSRNOG00000007431.9.
DR   AGR; RGD:1308066; -.
DR   RGD; 1308066; Shroom1.
DR   eggNOG; ENOG502SM3B; Eukaryota.
DR   GeneTree; ENSGT00940000160656; -.
DR   HOGENOM; CLU_016932_0_0_1; -.
DR   InParanoid; M0RB44; -.
DR   OrthoDB; 5266822at2759; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000007431; Expressed in liver and 12 other cell types or tissues.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR   GO; GO:0045159; F:myosin II binding; ISO:RGD.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISO:RGD.
DR   GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR   Gene3D; 6.10.250.3120; -; 1.
DR   InterPro; IPR014800; ASD1_dom.
DR   InterPro; IPR014799; ASD2_dom.
DR   InterPro; IPR027685; Shroom_fam.
DR   PANTHER; PTHR15012; APICAL PROTEIN/SHROOM-RELATED; 1.
DR   PANTHER; PTHR15012:SF37; PROTEIN SHROOM1; 1.
DR   Pfam; PF08688; ASD1; 1.
DR   Pfam; PF08687; ASD2; 1.
DR   PROSITE; PS51306; ASD1; 1.
DR   PROSITE; PS51307; ASD2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00637};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M0RB44};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          178..266
FT                   /note="ASD1"
FT                   /evidence="ECO:0000259|PROSITE:PS51306"
FT   DOMAIN          550..830
FT                   /note="ASD2"
FT                   /evidence="ECO:0000259|PROSITE:PS51307"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          757..784
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        28..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  92595 MW;  F7CEB5A232E0AF9F CRC64;
     HTETLTEWSG SRLGGTGSPP GPPTPVPNCT TMETTMGTGR DRTSQASDTE SLDLRRLSTR
     ADSAYSSFST ASGGPETRTP SPGTERLPYL DWDYVRVVWG NRSPISKDAV PSMTQGPGPA
     VVAGHSDPRP PEVQGNAGPL SRQDTPLLYA LTAEAEATTR TAEPPSPPAS RAAYRQRLQG
     AQRRVLRETS FQRKELRMSL PGRLRPALPA RPPTGHVRSA SSSQELGEAE PARAAVPALG
     AAGRGHLASQ QRLCCFSEPG KLHRVGWSGG PTGEGLREAY STQELQRGMH AKSKGLQETQ
     SLSSTELNSR SANLASAHRP AGRSQSVSGC TGSERTVATV QVVPQRADTP RPPLQTKLSR
     FLTQKEAAVV CPGEALQAKP AGCARRNPET TVSTPGPSLP DDEVFLKEAK TASPQDSHAP
     HGLPTSTSDR PSENGLSKKA GQITVSAERA LHEVPGIAGA DNCWQGVNGS VHISRPTSRS
     TPETTNDDTP TFDTNGTTDP SAATEKNPLK PPSVDVLTTS DSETPGSPHH ASLTWGQLGS
     KPTWPSRHFE ELVQELARLD PFLSDTLAAQ PGPEPPLGLL DGLFPAEEIR SAMRPAREEA
     GEKAGASEEG SCGCHFTQEL PTSQEASRSE NSTPDPVPDQ SSGQGFPEGN STQAKKVELA
     RLLQKMLQDL HAEQERLRGK AADWTRHNGA LEAAVSQACT PRELERFRRF MTDLERVLGL
     LLLLGSRLTR VNLALARAGS DSDPDERASL LQRLLLLQRQ QEDAKELKEH VARREQTLRQ
     VLERELPAEH LRSYCVLLAA KARILSQQRS LDDRIRFLKE QLDTIWSDLS HHPLSPRLSW
     APGIRPLDKQ PFLATLI
//
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