SHRM2_RAT
ID SHRM2_RAT Reviewed; 1423 AA.
AC Q7TP36;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein Shroom2;
DE AltName: Full=Liver regeneration-related protein LRRG167;
DE AltName: Full=Protein Apxl;
GN Name=Shroom2; Synonyms=Apxl; ORFNames=Ab2-404;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Yuan J.Y., Yang K.J., Yan H.M., Chang C.F.,
RA Zhao L.F., Ma H., Wang L., Wang S.F., Shi J.B., Rahman S., Wang Q.N.,
RA Zhang J.B., Han H.P., Wang G.P., Chai L.Q.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-185; SER-831;
RP SER-918; SER-920 AND SER-1329, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
CC -!- FUNCTION: May be involved in endothelial cell morphology changes during
CC cell spreading. In the retinal pigment epithelium, may regulate the
CC biogenesis of melanosomes and promote their association with the apical
CC cell surface by inducing gamma-tubulin redistribution (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}. Cell
CC junction, tight junction {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Associates with cortical F-actin. {ECO:0000250}.
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
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DR EMBL; AY325213; AAP92614.1; -; mRNA.
DR AlphaFoldDB; Q7TP36; -.
DR SMR; Q7TP36; -.
DR STRING; 10116.ENSRNOP00000056187; -.
DR iPTMnet; Q7TP36; -.
DR PhosphoSitePlus; Q7TP36; -.
DR SwissPalm; Q7TP36; -.
DR jPOST; Q7TP36; -.
DR PaxDb; Q7TP36; -.
DR PRIDE; Q7TP36; -.
DR Ensembl; ENSRNOT00000050819; ENSRNOP00000042259; ENSRNOG00000024322.
DR RGD; 1565163; Shroom2.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR GeneTree; ENSGT00940000155212; -.
DR InParanoid; Q7TP36; -.
DR PRO; PR:Q7TP36; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000024322; Expressed in Ammon's horn and 18 other tissues.
DR ExpressionAtlas; Q7TP36; baseline and differential.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0043296; C:apical junction complex; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0045217; P:cell-cell junction maintenance; ISO:RGD.
DR GO; GO:0032401; P:establishment of melanosome localization; IEA:InterPro.
DR GO; GO:0032438; P:melanosome organization; ISS:UniProtKB.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; ISO:RGD.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR027686; Shroom2.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 2.
DR PANTHER; PTHR15012:SF8; PTHR15012:SF8; 2.
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; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Developmental protein; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome; Tight junction.
FT CHAIN 1..1423
FT /note="Protein Shroom2"
FT /id="PRO_0000286064"
FT DOMAIN 575..677
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1092..1418
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1069
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13796"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 834
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1072
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1423 AA; 157989 MW; 13E5176B51C333C9 CRC64;
MRPSTVTSRI WWSESSSSSS HDLSGSWEHT SLQRTSDHFS SMGSIDSLDH SSQLYPSGHL
SSAKSNSSID HLGGHSKRDS AYGSFSTCSS TPDHTLPKAD ASSTENILYK VGLWEASRPG
SSRQSQSTGD PQGLQDRPSS FLPRVPGNSS KSPRPEDNIE PKIATSGRSN FGPVWYVPDK
KKAPSPPPLG LPLRSDSFAV AARGHEKARG PPFSDLASMQ HFTTLPHVQP RGDRRMETTD
RQWKLAHPSS GKEIGNVGYQ PEGHLDCRWL CSDDRAGRPS GAPGRHQFSL SSTDVHFLKS
YHGSQHPQPC SDESPRFPSS PRELLRITPS GCLQEPPELS QDDNPAQVRW PGSVNQKLDD
RGRSHYFSVP HRQPVHGSAH VLIPRSDYWH SDTTPVDLEC PLLRPDQRGY PQQYEETPAS
HERGGYQQLN AGIEGCCSGI HEPPRASHTV RAGLQCPGND FKLVDAESGR ISRQRTPMLH
SLTQDGAWRP GNSKDCGNEK PPLLDAQVGK PTRRSDRFAT TLRNEIQMRR AKLQKSKSTV
TLAGDSEAED CAGDWRVDVG AVPEGSFPST YKEHLKEAQT RVLKATSFQR RDLDPTPADQ
YPGPPEHRTC DHSASSSLSS FPGEPDSAPR LCEAGLAKPP SSAGGVPHIL RIGGRKRFTA
EQKLKSYSEP EKINEVGLSG DHSPHPTIRT SEDSVGTFAD RWKFFEETSK SLLQKPGHRQ
AFCGIPREKA ERPQTQGHEC ESTEPWFQKR SRATSCGEIL SEDRKVEKAS EKLNPPRRLG
TFAEYQASWK EQKKSLEARS SGRYHSADDI LDAGLDQQQR PQYIHERSRS SPSTDHYSQE
VPVEPNRQAE DSGGQKEALL CTLQAEEGCS APSSSVLSSA QPQDSQHVNE DPTSPQPEAQ
LSSKCQHLQT STMETSRSPS PQFAPQKLTD KPPLLIHEDN SARYCPVTAC YVFIPCRLQV
FVAGALPQLQ TLGIERVMDN NTTVKMVPIK IVHSESQPEK ESRQSLACPA ELPALPSGLE
KDQIKTLSTS EQCYSRFCVY TRQEVETPHR ARPPEPQPPS TPAPPVRDSC SSPPSLNYGK
AKEKTVDDLK SEELAREIVG KDKSLADILD PSVKIKTTMD LMEGIFPKDE YLLEEAQQRR
KLLPKVPSPR VTEDNSCPSL SAICYNLGTR SKSVPVSQLI KIKILASSPR KQDPGMPGVV
SLATNSTYYS TSAPKAELLI KMKDLQEPEE YSAGDLDHDL SIKKQELIDS ISRKLQVLRE
ARESLLEDIQ ANNALGDEVE AIVKDVCKPN EFDKFRMFIG DLDKVVNLLL SLSGRLARVE
NALNNLDDSP SPGDRQSLLE KQRVLTQQHE DAKELKENLD RRERIVFDIL ATYLSEENLA
DYEHFVKMKS ALIIEQRELE DKIHLGEEQL KCLFDSLQPE RSK
