SHRM3_XENLA
ID SHRM3_XENLA Reviewed; 1788 AA.
AC Q27IV2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Protein Shroom3;
DE AltName: Full=Shroom-like protein;
GN Name=shroom3; Synonyms=shrm;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=17329357; DOI=10.1242/dev.02828;
RA Lee C., Scherr H.M., Wallingford J.B.;
RT "Shroom family proteins regulate gamma-tubulin distribution and microtubule
RT architecture during epithelial cell shape change.";
RL Development 134:1431-1441(2007).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14680628; DOI=10.1016/j.cub.2003.11.054;
RA Haigo S.L., Hildebrand J.D., Harland R.M., Wallingford J.B.;
RT "Shroom induces apical constriction and is required for hingepoint
RT formation during neural tube closure.";
RL Curr. Biol. 13:2125-2137(2003).
RN [3]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V.,
RA Smith P., Staub O., Hildebrand J.D., Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
CC -!- FUNCTION: Controls cell shape changes in the neuroepithelium during
CC neural tube closure (PubMed:14680628). Induces apical constriction in
CC epithelial cells by promoting the apical accumulation of F-actin and
CC myosin II, and probably by bundling stress fibers (PubMed:14680628).
CC Induces apicobasal cell elongation by redistributing gamma-tubulin and
CC directing the assembly of robust apicobasal microtubule arrays
CC (PubMed:17329357). {ECO:0000269|PubMed:14680628,
CC ECO:0000269|PubMed:17329357}.
CC -!- SUBUNIT: Interacts with F-actin. Interacts with ROCK1.
CC {ECO:0000250|UniProtKB:Q9QXN0}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q9QXN0}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9QXN0}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9QXN0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9QXN0}. Note=Colocalizes with F-actin in stress
CC fibers and adherens junctions. {ECO:0000250|UniProtKB:Q9QXN0}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells of the cement gland.
CC {ECO:0000269|PubMed:17329357}.
CC -!- DEVELOPMENTAL STAGE: Expresseion initiates in the anterior neural plate
CC and extends posteriorly as neurulation proceeds. At the end of
CC neurulation, expressed in the otic and nasal placodes.
CC {ECO:0000269|PubMed:14680628}.
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}.
CC -!- DOMAIN: The ASD2 domain mediates the interaction with ROCK1 and is
CC required for apical constriction induction.
CC {ECO:0000250|UniProtKB:Q9QXN0}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
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DR EMBL; DQ398586; ABD59319.1; -; mRNA.
DR RefSeq; NP_001089158.1; NM_001095689.1.
DR PRIDE; Q27IV2; -.
DR GeneID; 734194; -.
DR KEGG; xla:734194; -.
DR CTD; 734194; -.
DR Xenbase; XB-GENE-490228; shroom3.L.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 734194; Expressed in heart and 14 other tissues.
DR GO; GO:0005912; C:adherens junction; ISS:HGNC-UCL.
DR GO; GO:0016324; C:apical plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; ISS:HGNC-UCL.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; ISS:HGNC-UCL.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045176; P:apical protein localization; IDA:HGNC-UCL.
DR GO; GO:0000902; P:cell morphogenesis; IMP:HGNC-UCL.
DR GO; GO:0043482; P:cellular pigment accumulation; IMP:HGNC-UCL.
DR GO; GO:0002064; P:epithelial cell development; IEA:InterPro.
DR GO; GO:0001843; P:neural tube closure; IEA:InterPro.
DR GO; GO:0007389; P:pattern specification process; ISS:HGNC-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR030494; Shrm3.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR PANTHER; PTHR15012:SF33; PTHR15012:SF33; 1.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell junction; Cell membrane; Cell shape; Coiled coil;
KW Cytoplasm; Cytoskeleton; Developmental protein; Membrane; Microtubule;
KW Reference proteome.
FT CHAIN 1..1788
FT /note="Protein Shroom3"
FT /id="PRO_0000286068"
FT DOMAIN 708..811
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1467..1756
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1653..1708
FT /evidence="ECO:0000255"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1788 AA; 200726 MW; 9660CB8BEE090784 CRC64;
MMQVSQGTIG SPWHQAYHSS SSTSDLSGYN HEFLRRSPDQ YSSRGSMESL DQASAAYHHH
LPPAKSTNCI DQLVHLHNKR DSAYSSFSTN ASIPEYRSSP FSKERSYSME SMHSRNSSGQ
EGIKHADIKY IKTVYDVQRG ISEEYEVNSS SVKNRNYSRQ PAYNRHSIGP HGRLEQSRFF
SESGGFERAA PMPPTRSDSY ALTRHHERPN SWSSLDQNRN FRTPKAAGLH STNTSSNAAQ
QPKHVHGDGH LHPVLERSPE SSPLIKPKQV YSETPQPGQP MLPTGIYPVP APEPHFAHAP
QPPKNNNGRL YPALAKEGSY GAKSSEKVLP FSEPNKNEKD TQNLRSKSVG QYPMNHSVKE
REKKQEGPTG FAHYKLHFTA GPDISTSSLT NDRNDQQPLR LDNIDINEQQ KNGTKVAEEF
SVYAHPAFQN EWSDSKTKQD IASSDIIGLH RNSLSSDAHG EHEYHNHFNI ASSSHNKMDE
RSNRQADHRK KLESLSFTVH ADEADGPSSN PLKPDESPSP SQKKSYDFTR RRLSSSSSQS
SKTDGNKLSS VFDKVCKIEQ REHENHRSQF LCGNINQSGL STRGQNNKGS FTMVEEIRNK
FISQDQTPNP NEWRRLSSSH SNEKVTGMHQ LTRQGIVYGL QTGDAQKQMP EKQAEKMHSY
NQEQNILQAV PDDDNRSFNS QTMPNKEDDW QCAAQDTLGF NRAYRNSVKD AQCKVLEATS
YRRKDLEISP PHYKKPEKNV RPASAPFRKK SSSLSPHAPK ERHSVTPTDN CASIQESQGV
FFPSRIGAKR RITAEQKKRS YSEPEKMNEV GASESESAPL TVSKMEPVAS FSENSVADRR
RIFEREGKAC STINLSKPQL KQLQQNALAD YIERKTGRRP SSQETRLLKE RSQSTYFSGS
IMDNQSMTST SSMNSLNEHN LSYRHREPLS KTGRVSSTLP PGLTGFFDLS SFENNPEYPE
NRSRSSSFAH QLRSERLLDH RSKVEFGKGR ETNKPKEVSL QSDDDVIITS SRRHGKSASA
EDLLDRLPQP PALHVRSRSS PASDMKSREY MSRQEVGNKT SYASASNKEI RSIKSNHFEQ
MSFTPSFKNH IDTGEDPVPE NSSTIQRSAQ LENQRNTKTQ SISGIYSPHP ETKQEPLALP
IHSVPAKVTQ TSLAHATFDY ITAEEYLYSG KRGKESASPT DNKEISDQEW CLPENSSSED
LNDPERFAKY TSAQRPQSFE TKSGNSINET VQQNKSSGPT AGPKFSTSWK SNGMWSSGSS
EAETTFNHGK ISLHISESCL QPQSPMTGQE DEGDDEVFVK EQDTESFSGT FVPPSPPPFP
PPSLEDALLK QRIEKFPLVP NTLDEIWENT EEASTQVKVK SNERYLQCAS EYTASTESSG
SYLLNSGITK RDTDGPLLRL SSIVPAPEPL ASPVDPTKPI EEQETQPHGA DTSILQSSEG
NFNPSDSQST LPHVRSELMS SEDAKSQELA KEIVTKDKSL ANILDPDSRM KTTMDLMEGL
FTKSSSALKE KNQKRKAKKQ IDNIIAPESE XKEEKRETLD NASNYSAYYS TSAPKAELLR
KMKTIHSQIG GKEEQFDVNE KKAELISSLT CKLEVLKDAK ESLIDDIKLN NSLGEEVETQ
IETLCKPNEF DKYKMFIGDL DKVVNLLLSL SGRLARVENA LSSLGEDASA EERKTWNEKK
KQLCGQHEDA RELKENLDRR EKLVMDFLGN YLTGEEFAHY QHFVKMKSAL LIEQRELDDK
IKLGQEQLRC LTESLPSDYL ISMKVSLPEE RRSSLGNKSL PPPLTSSL
