Full text data of SHROOM3
SHROOM3
(KIAA1481, SHRML)
[Confidence: low (only semi-automatic identification from reviews)]
Protein Shroom3 (Shroom-related protein; hShrmL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein Shroom3 (Shroom-related protein; hShrmL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8TF72
ID SHRM3_HUMAN Reviewed; 1996 AA.
AC Q8TF72; Q5QTQ3; Q6ZRW3; Q96IR9; Q9P247;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-JUL-2010, sequence version 2.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Protein Shroom3;
DE AltName: Full=Shroom-related protein;
DE Short=hShrmL;
GN Name=SHROOM3; Synonyms=KIAA1481, SHRML; ORFNames=MSTP013;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-279; ALA-469
RP AND LEU-1290.
RA Koide M., Iio A., Obata K., Inagaki M., Yokota M., Ono T., Tuan R.S.;
RT "Molecular cloning of FKBP12-associated protein.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-1996 (ISOFORM 1), AND
RP VARIANT LEU-1290.
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1230-1996 (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1799-1996 (ISOFORM 1).
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P.,
RA Schiaffino M.V., Smith P., Staub O., Hildebrand J.D.,
RA Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-913, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-443; SER-910;
RP SER-913 AND SER-1221, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-970, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Controls cell shape changes in the neuroepithelium
CC during neural tube closure. Induces apical constriction in
CC epithelial cells by promoting the apical accumulation of F-actin
CC and myosin II, and probably by bundling stress fibers. Induces
CC apicobasal cell elongation by redistributing gamma-tubulin and
CC directing the assembly of robust apicobasal microtubule arrays (By
CC similarity).
CC -!- SUBUNIT: Interacts with F-actin (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction (By
CC similarity). Cytoplasm, cytoskeleton (By similarity).
CC Note=Colocalizes with F-actin in stress fibers and adherens
CC junctions (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TF72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TF72-2; Sequence=VSP_024965, VSP_024966, VSP_024967,
CC VSP_024968;
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding (By similarity).
CC -!- DOMAIN: The ASD2 domain is required for apical constriction
CC induction (By similarity).
CC -!- SIMILARITY: Belongs to the shroom family.
CC -!- SIMILARITY: Contains 1 ASD1 domain.
CC -!- SIMILARITY: Contains 1 ASD2 domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC Met-2 is more conserved than Met-1 among the orthologs.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13515.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB84689.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB055660; BAB84689.1; ALT_INIT; mRNA.
DR EMBL; AK127929; BAC87195.1; -; mRNA.
DR EMBL; AC096743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040914; BAA96005.1; -; mRNA.
DR EMBL; BC007291; AAH07291.1; -; mRNA.
DR EMBL; AF109367; AAQ13515.1; ALT_INIT; mRNA.
DR RefSeq; NP_065910.3; NM_020859.3.
DR RefSeq; XP_005263219.1; XM_005263162.1.
DR UniGene; Hs.702168; -.
DR ProteinModelPortal; Q8TF72; -.
DR SMR; Q8TF72; 25-108, 1779-1955.
DR IntAct; Q8TF72; 6.
DR MINT; MINT-2812419; -.
DR STRING; 9606.ENSP00000296043; -.
DR PhosphoSite; Q8TF72; -.
DR DMDM; 300669666; -.
DR PaxDb; Q8TF72; -.
DR PRIDE; Q8TF72; -.
DR Ensembl; ENST00000296043; ENSP00000296043; ENSG00000138771.
DR GeneID; 57619; -.
DR KEGG; hsa:57619; -.
DR UCSC; uc003hkf.1; human.
DR CTD; 57619; -.
DR GeneCards; GC04P077356; -.
DR H-InvDB; HIX0004309; -.
DR H-InvDB; HIX0163999; -.
DR HGNC; HGNC:30422; SHROOM3.
DR HPA; HPA047784; -.
DR MIM; 604570; gene.
DR neXtProt; NX_Q8TF72; -.
DR PharmGKB; PA147357295; -.
DR eggNOG; NOG72784; -.
DR HOGENOM; HOG000169233; -.
DR HOVERGEN; HBG108489; -.
DR InParanoid; Q8TF72; -.
DR OMA; HTPRERH; -.
DR OrthoDB; EOG7QZG8T; -.
DR ChiTaRS; SHROOM3; human.
DR GeneWiki; SHROOM3; -.
DR GenomeRNAi; 57619; -.
DR NextBio; 64290; -.
DR PRO; PR:Q8TF72; -.
DR Bgee; Q8TF72; -.
DR CleanEx; HS_SHROOM3; -.
DR Genevestigator; Q8TF72; -.
DR GO; GO:0005912; C:adherens junction; ISS:HGNC.
DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:HGNC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; ISS:HGNC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0045176; P:apical protein localization; ISS:HGNC.
DR GO; GO:0000902; P:cell morphogenesis; ISS:HGNC.
DR GO; GO:0043482; P:cellular pigment accumulation; ISS:HGNC.
DR GO; GO:0002066; P:columnar/cuboidal epithelial cell development; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; ISS:HGNC.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR014800; ASD1.
DR InterPro; IPR014799; ASD2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell shape;
KW Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
KW Microtubule; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1996 Protein Shroom3.
FT /FTId=PRO_0000286066.
FT DOMAIN 25 110 PDZ.
FT DOMAIN 928 1030 ASD1.
FT DOMAIN 1669 1957 ASD2.
FT MOD_RES 439 439 Phosphoserine.
FT MOD_RES 443 443 Phosphoserine.
FT MOD_RES 910 910 Phosphoserine.
FT MOD_RES 913 913 Phosphoserine.
FT MOD_RES 970 970 Phosphoserine.
FT MOD_RES 1221 1221 Phosphoserine.
FT VAR_SEQ 1 125 Missing (in isoform 2).
FT /FTId=VSP_024965.
FT VAR_SEQ 126 153 SPEHLTSGPQHRKAAWSGGVKLRLKHRR -> MAFYSTPEY
FT DIQLARGLLSGMFLFATRR (in isoform 2).
FT /FTId=VSP_024966.
FT VAR_SEQ 277 311 ISGRERSGSMDNTSARGGLLEGMRQADIRYVKTVY -> KR
FT VKTRDLPGSQSPGRAISRKTTMPTSGGGWREKA (in
FT isoform 2).
FT /FTId=VSP_024967.
FT VAR_SEQ 312 1996 Missing (in isoform 2).
FT /FTId=VSP_024968.
FT VARIANT 147 147 L -> H (in dbSNP:rs3821979).
FT /FTId=VAR_032062.
FT VARIANT 279 279 G -> A (in dbSNP:rs344140).
FT /FTId=VAR_032063.
FT VARIANT 469 469 P -> A (in dbSNP:rs344141).
FT /FTId=VAR_032064.
FT VARIANT 1290 1290 P -> L (in dbSNP:rs3733242).
FT /FTId=VAR_032065.
FT CONFLICT 153 153 R -> S (in Ref. 1; BAB84689).
SQ SEQUENCE 1996 AA; 216857 MW; 735F6CD20FF64BC6 CRC64;
MMRTTEDFHK PSATLNSNTA TKGRYIYLEA FLEGGAPWGF TLKGGLEHGE PLIISKVEEG
GKADTLSSKL QAGDEVVHIN EVTLSSSRKE AVSLVKGSYK TLRLVVRRDV CTDPGHADTG
ASNFVSPEHL TSGPQHRKAA WSGGVKLRLK HRRSEPAGRP HSWHTTKSGE KQPDASMMQI
SQGMIGPPWH QSYHSSSSTS DLSNYDHAYL RRSPDQCSSQ GSMESLEPSG AYPPCHLSPA
KSTGSIDQLS HFHNKRDSAY SSFSTSSSIL EYPHPGISGR ERSGSMDNTS ARGGLLEGMR
QADIRYVKTV YDTRRGVSAE YEVNSSALLL QGREARASAN GQGYDKWSNI PRGKGVPPPS
WSQQCPSSLE TATDNLPPKV GAPLPPARSD SYAAFRHRER PSSWSSLDQK RLCRPQANSL
GSLKSPFIEE QLHTVLEKSP ENSPPVKPKH NYTQKAQPGQ PLLPTSIYPV PSLEPHFAQV
PQPSVSSNGM LYPALAKESG YIAPQGACNK MATIDENGNQ NGSGRPGFAF CQPLEHDLLS
PVEKKPEATA KYVPSKVHFC SVPENEEDAS LKRHLTPPQG NSPHSNERKS THSNKPSSHP
HSLKCPQAQA WQAGEDKRSS RLSEPWEGDF QEDHNANLWR RLEREGLGQS LSGNFGKTKS
AFSSLQNIPE SLRRHSSLEL GRGTQEGYPG GRPTCAVNTK AEDPGRKAAP DLGSHLDRQV
SYPRPEGRTG ASASFNSTDP SPEEPPAPSH PHTSSLGRRG PGPGSASALQ GFQYGKPHCS
VLEKVSKFEQ REQGSQRPSV GGSGFGHNYR PHRTVSTSST SGNDFEETKA HIRFSESAEP
LGNGEQHFKN GELKLEEASR QPCGQQLSGG ASDSGRGPQR PDARLLRSQS TFQLSSEPER
EPEWRDRPGS PESPLLDAPF SRAYRNSIKD AQSRVLGATS FRRRDLELGA PVASRSWRPR
PSSAHVGLRS PEASASASPH TPRERHSVTP AEGDLARPVP PAARRGARRR LTPEQKKRSY
SEPEKMNEVG IVEEAEPAPL GPQRNGMRFP ESSVADRRRL FERDGKACST LSLSGPELKQ
FQQSALADYI QRKTGKRPTS AAGCSLQEPG PLRERAQSAY LQPGPAALEG SGLASASSLS
SLREPSLQPR REATLLPATV AETQQAPRDR SSSFAGGRRL GERRRGDLLS GANGGTRGTQ
RGDETPREPS SWGARAGKSM SAEDLLERSD VLAGPVHVRS RSSPATADKR QDVLLGQDSG
FGLVKDPCYL AGPGSRSLSC SERGQEEMLP LFHHLTPRWG GSGCKAIGDS SVPSECPGTL
DHQRQASRTP CPRPPLAGTQ GLVTDTRAAP LTPIGTPLPS AIPSGYCSQD GQTGRQPLPP
YTPAMMHRSN GHTLTQPPGP RGCEGDGPEH GVEEGTRKRV SLPQWPPPSR AKWAHAARED
SLPEESSAPD FANLKHYQKQ QSLPSLCSTS DPDTPLGAPS TPGRISLRIS ESVLRDSPPP
HEDYEDEVFV RDPHPKATSS PTFEPLPPPP PPPPSQETPV YSMDDFPPPP PHTVCEAQLD
SEDPEGPRPS FNKLSKVTIA RERHMPGAAH VVGSQTLASR LQTSIKGSEA ESTPPSFMSV
HAQLAGSLGG QPAPIQTQSL SHDPVSGTQG LEKKVSPDPQ KSSEDIRTEA LAKEIVHQDK
SLADILDPDS RLKTTMDLME GLFPRDVNLL KENSVKRKAI QRTVSSSGCE GKRNEDKEAV
SMLVNCPAYY SVSAPKAELL NKIKEMPAEV NEEEEQADVN EKKAELIGSL THKLETLQEA
KGSLLTDIKL NNALGEEVEA LISELCKPNE FDKYRMFIGD LDKVVNLLLS LSGRLARVEN
VLSGLGEDAS NEERSSLYEK RKILAGQHED ARELKENLDR RERVVLGILA NYLSEEQLQD
YQHFVKMKST LLIEQRKLDD KIKLGQEQVK CLLESLPSDF IPKAGALALP PNLTSEPIPA
GGCTFSGIFP TLTSPL
//
ID SHRM3_HUMAN Reviewed; 1996 AA.
AC Q8TF72; Q5QTQ3; Q6ZRW3; Q96IR9; Q9P247;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-JUL-2010, sequence version 2.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Protein Shroom3;
DE AltName: Full=Shroom-related protein;
DE Short=hShrmL;
GN Name=SHROOM3; Synonyms=KIAA1481, SHRML; ORFNames=MSTP013;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-279; ALA-469
RP AND LEU-1290.
RA Koide M., Iio A., Obata K., Inagaki M., Yokota M., Ono T., Tuan R.S.;
RT "Molecular cloning of FKBP12-associated protein.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-1996 (ISOFORM 1), AND
RP VARIANT LEU-1290.
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1230-1996 (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1799-1996 (ISOFORM 1).
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P.,
RA Schiaffino M.V., Smith P., Staub O., Hildebrand J.D.,
RA Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-913, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-443; SER-910;
RP SER-913 AND SER-1221, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-970, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Controls cell shape changes in the neuroepithelium
CC during neural tube closure. Induces apical constriction in
CC epithelial cells by promoting the apical accumulation of F-actin
CC and myosin II, and probably by bundling stress fibers. Induces
CC apicobasal cell elongation by redistributing gamma-tubulin and
CC directing the assembly of robust apicobasal microtubule arrays (By
CC similarity).
CC -!- SUBUNIT: Interacts with F-actin (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction (By
CC similarity). Cytoplasm, cytoskeleton (By similarity).
CC Note=Colocalizes with F-actin in stress fibers and adherens
CC junctions (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TF72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TF72-2; Sequence=VSP_024965, VSP_024966, VSP_024967,
CC VSP_024968;
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding (By similarity).
CC -!- DOMAIN: The ASD2 domain is required for apical constriction
CC induction (By similarity).
CC -!- SIMILARITY: Belongs to the shroom family.
CC -!- SIMILARITY: Contains 1 ASD1 domain.
CC -!- SIMILARITY: Contains 1 ASD2 domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC Met-2 is more conserved than Met-1 among the orthologs.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13515.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB84689.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB055660; BAB84689.1; ALT_INIT; mRNA.
DR EMBL; AK127929; BAC87195.1; -; mRNA.
DR EMBL; AC096743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040914; BAA96005.1; -; mRNA.
DR EMBL; BC007291; AAH07291.1; -; mRNA.
DR EMBL; AF109367; AAQ13515.1; ALT_INIT; mRNA.
DR RefSeq; NP_065910.3; NM_020859.3.
DR RefSeq; XP_005263219.1; XM_005263162.1.
DR UniGene; Hs.702168; -.
DR ProteinModelPortal; Q8TF72; -.
DR SMR; Q8TF72; 25-108, 1779-1955.
DR IntAct; Q8TF72; 6.
DR MINT; MINT-2812419; -.
DR STRING; 9606.ENSP00000296043; -.
DR PhosphoSite; Q8TF72; -.
DR DMDM; 300669666; -.
DR PaxDb; Q8TF72; -.
DR PRIDE; Q8TF72; -.
DR Ensembl; ENST00000296043; ENSP00000296043; ENSG00000138771.
DR GeneID; 57619; -.
DR KEGG; hsa:57619; -.
DR UCSC; uc003hkf.1; human.
DR CTD; 57619; -.
DR GeneCards; GC04P077356; -.
DR H-InvDB; HIX0004309; -.
DR H-InvDB; HIX0163999; -.
DR HGNC; HGNC:30422; SHROOM3.
DR HPA; HPA047784; -.
DR MIM; 604570; gene.
DR neXtProt; NX_Q8TF72; -.
DR PharmGKB; PA147357295; -.
DR eggNOG; NOG72784; -.
DR HOGENOM; HOG000169233; -.
DR HOVERGEN; HBG108489; -.
DR InParanoid; Q8TF72; -.
DR OMA; HTPRERH; -.
DR OrthoDB; EOG7QZG8T; -.
DR ChiTaRS; SHROOM3; human.
DR GeneWiki; SHROOM3; -.
DR GenomeRNAi; 57619; -.
DR NextBio; 64290; -.
DR PRO; PR:Q8TF72; -.
DR Bgee; Q8TF72; -.
DR CleanEx; HS_SHROOM3; -.
DR Genevestigator; Q8TF72; -.
DR GO; GO:0005912; C:adherens junction; ISS:HGNC.
DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:HGNC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; ISS:HGNC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0045176; P:apical protein localization; ISS:HGNC.
DR GO; GO:0000902; P:cell morphogenesis; ISS:HGNC.
DR GO; GO:0043482; P:cellular pigment accumulation; ISS:HGNC.
DR GO; GO:0002066; P:columnar/cuboidal epithelial cell development; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; ISS:HGNC.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR014800; ASD1.
DR InterPro; IPR014799; ASD2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell shape;
KW Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
KW Microtubule; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1996 Protein Shroom3.
FT /FTId=PRO_0000286066.
FT DOMAIN 25 110 PDZ.
FT DOMAIN 928 1030 ASD1.
FT DOMAIN 1669 1957 ASD2.
FT MOD_RES 439 439 Phosphoserine.
FT MOD_RES 443 443 Phosphoserine.
FT MOD_RES 910 910 Phosphoserine.
FT MOD_RES 913 913 Phosphoserine.
FT MOD_RES 970 970 Phosphoserine.
FT MOD_RES 1221 1221 Phosphoserine.
FT VAR_SEQ 1 125 Missing (in isoform 2).
FT /FTId=VSP_024965.
FT VAR_SEQ 126 153 SPEHLTSGPQHRKAAWSGGVKLRLKHRR -> MAFYSTPEY
FT DIQLARGLLSGMFLFATRR (in isoform 2).
FT /FTId=VSP_024966.
FT VAR_SEQ 277 311 ISGRERSGSMDNTSARGGLLEGMRQADIRYVKTVY -> KR
FT VKTRDLPGSQSPGRAISRKTTMPTSGGGWREKA (in
FT isoform 2).
FT /FTId=VSP_024967.
FT VAR_SEQ 312 1996 Missing (in isoform 2).
FT /FTId=VSP_024968.
FT VARIANT 147 147 L -> H (in dbSNP:rs3821979).
FT /FTId=VAR_032062.
FT VARIANT 279 279 G -> A (in dbSNP:rs344140).
FT /FTId=VAR_032063.
FT VARIANT 469 469 P -> A (in dbSNP:rs344141).
FT /FTId=VAR_032064.
FT VARIANT 1290 1290 P -> L (in dbSNP:rs3733242).
FT /FTId=VAR_032065.
FT CONFLICT 153 153 R -> S (in Ref. 1; BAB84689).
SQ SEQUENCE 1996 AA; 216857 MW; 735F6CD20FF64BC6 CRC64;
MMRTTEDFHK PSATLNSNTA TKGRYIYLEA FLEGGAPWGF TLKGGLEHGE PLIISKVEEG
GKADTLSSKL QAGDEVVHIN EVTLSSSRKE AVSLVKGSYK TLRLVVRRDV CTDPGHADTG
ASNFVSPEHL TSGPQHRKAA WSGGVKLRLK HRRSEPAGRP HSWHTTKSGE KQPDASMMQI
SQGMIGPPWH QSYHSSSSTS DLSNYDHAYL RRSPDQCSSQ GSMESLEPSG AYPPCHLSPA
KSTGSIDQLS HFHNKRDSAY SSFSTSSSIL EYPHPGISGR ERSGSMDNTS ARGGLLEGMR
QADIRYVKTV YDTRRGVSAE YEVNSSALLL QGREARASAN GQGYDKWSNI PRGKGVPPPS
WSQQCPSSLE TATDNLPPKV GAPLPPARSD SYAAFRHRER PSSWSSLDQK RLCRPQANSL
GSLKSPFIEE QLHTVLEKSP ENSPPVKPKH NYTQKAQPGQ PLLPTSIYPV PSLEPHFAQV
PQPSVSSNGM LYPALAKESG YIAPQGACNK MATIDENGNQ NGSGRPGFAF CQPLEHDLLS
PVEKKPEATA KYVPSKVHFC SVPENEEDAS LKRHLTPPQG NSPHSNERKS THSNKPSSHP
HSLKCPQAQA WQAGEDKRSS RLSEPWEGDF QEDHNANLWR RLEREGLGQS LSGNFGKTKS
AFSSLQNIPE SLRRHSSLEL GRGTQEGYPG GRPTCAVNTK AEDPGRKAAP DLGSHLDRQV
SYPRPEGRTG ASASFNSTDP SPEEPPAPSH PHTSSLGRRG PGPGSASALQ GFQYGKPHCS
VLEKVSKFEQ REQGSQRPSV GGSGFGHNYR PHRTVSTSST SGNDFEETKA HIRFSESAEP
LGNGEQHFKN GELKLEEASR QPCGQQLSGG ASDSGRGPQR PDARLLRSQS TFQLSSEPER
EPEWRDRPGS PESPLLDAPF SRAYRNSIKD AQSRVLGATS FRRRDLELGA PVASRSWRPR
PSSAHVGLRS PEASASASPH TPRERHSVTP AEGDLARPVP PAARRGARRR LTPEQKKRSY
SEPEKMNEVG IVEEAEPAPL GPQRNGMRFP ESSVADRRRL FERDGKACST LSLSGPELKQ
FQQSALADYI QRKTGKRPTS AAGCSLQEPG PLRERAQSAY LQPGPAALEG SGLASASSLS
SLREPSLQPR REATLLPATV AETQQAPRDR SSSFAGGRRL GERRRGDLLS GANGGTRGTQ
RGDETPREPS SWGARAGKSM SAEDLLERSD VLAGPVHVRS RSSPATADKR QDVLLGQDSG
FGLVKDPCYL AGPGSRSLSC SERGQEEMLP LFHHLTPRWG GSGCKAIGDS SVPSECPGTL
DHQRQASRTP CPRPPLAGTQ GLVTDTRAAP LTPIGTPLPS AIPSGYCSQD GQTGRQPLPP
YTPAMMHRSN GHTLTQPPGP RGCEGDGPEH GVEEGTRKRV SLPQWPPPSR AKWAHAARED
SLPEESSAPD FANLKHYQKQ QSLPSLCSTS DPDTPLGAPS TPGRISLRIS ESVLRDSPPP
HEDYEDEVFV RDPHPKATSS PTFEPLPPPP PPPPSQETPV YSMDDFPPPP PHTVCEAQLD
SEDPEGPRPS FNKLSKVTIA RERHMPGAAH VVGSQTLASR LQTSIKGSEA ESTPPSFMSV
HAQLAGSLGG QPAPIQTQSL SHDPVSGTQG LEKKVSPDPQ KSSEDIRTEA LAKEIVHQDK
SLADILDPDS RLKTTMDLME GLFPRDVNLL KENSVKRKAI QRTVSSSGCE GKRNEDKEAV
SMLVNCPAYY SVSAPKAELL NKIKEMPAEV NEEEEQADVN EKKAELIGSL THKLETLQEA
KGSLLTDIKL NNALGEEVEA LISELCKPNE FDKYRMFIGD LDKVVNLLLS LSGRLARVEN
VLSGLGEDAS NEERSSLYEK RKILAGQHED ARELKENLDR RERVVLGILA NYLSEEQLQD
YQHFVKMKST LLIEQRKLDD KIKLGQEQVK CLLESLPSDF IPKAGALALP PNLTSEPIPA
GGCTFSGIFP TLTSPL
//
MIM
604570
*RECORD*
*FIELD* NO
604570
*FIELD* TI
*604570 SHROOM FAMILY MEMBER 3; SHROOM3
;;SHROOM, MOUSE, HOMOLOG OF; SHRM;;
KIAA1481
read more*FIELD* TX
CLONING
Using gene trap mutagenesis, Hildebrand and Soriano (1999) identified a
mutation in mice that caused exencephaly, acrania, facial clefting, and
spina bifida, all of which could be attributed to failed neural tube
closure. This mutation was designated 'shroom' (shrm), because the
neural folds 'mushroom' outward and do not converge at the dorsal
midline. By 5-prime RACE and library screening, the cDNA for the trapped
gene was cloned. Sequence analysis indicated there are at least 2 shrm
transcripts that encode 2 different putative protein products. The
longest predicted transcript, shrmL, encodes a protein of 1,986 amino
acids, while the second transcript, shrmS, encodes a protein of 1,808
amino acids that lacks the N-terminal 177 amino acids of shrmL. Shrm is
a PDZ domain-containing protein related to Xenopus Apx and human APXL
(SHROOM2; 300103).
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned SHRM, which they designated
KIAA1481. The deduced protein shares significant identity with human
APXL. RT-PCR ELISA detected highest expression of SHRM in liver,
followed by kidney, ovary, cerebellum, and spinal cord. Intermediate
expression was found in all other tissues and brain regions examined
except skeletal muscle, where there was little to no expression.
GENE FUNCTION
Hildebrand and Soriano (1999) found that Shrm is involved at several
levels in regulating aspects of cytoarchitecture. First, endogenous shrm
localized to adherens junctions and the cytoskeleton. Second,
ectopically expressed Shrm altered the subcellular distribution of
F-actin. Third, Shrm directly bound F-actin. Finally, cytoskeletal
polarity within the neuroepithelium was perturbed in mutant embryos. In
concert, these observations suggested that Shrm is a critical
determinant of the cellular architecture required for proper
neurulation.
In experiments in Xenopus, Lee et al. (2007) showed that SHROOM3 is
necessary and sufficient to induce a redistribution of the microtubule
regulator gamma-tubulin (see 191135). They found that this change in
gamma-tubulin distribution underlies the assembly of aligned arrays of
microtubules that drive apicobasal cell elongation. They concluded that
Shroom family proteins govern epithelial cell behaviors by coordinating
the assembly of both microtubule and actin cytoskeletons.
Hildebrand (2005) found that Shroom localized to the apical junctional
complex in Madin-Darby canine kidney cells. Overexpression of Shroom
resulted in altered cell morphology with apical constriction and altered
apical cell-cell alignment. Targeting the C-terminal domain of Shroom to
the apical plasma membrane produced similar changes. The neural
epithelia of Schroom-mutant mouse embryos showed a marked reduction in
the apical position of myosin IIB (MYH10; 160776), whereas the positions
of nectin-3 (PVRL3; 607147) and Zo1 (TJP1; 601009) were unaltered.
Hildebrand (2005) concluded that Shroom facilitates the subapical
distribution of nonmuscle myosin IIB, which in turn regulates the tissue
rigidity and cell shape changes required for neural tube closure.
MAPPING
By analyzing a human-rodent hybrid panel, Nagase et al. (2000) mapped
the SHRM gene to chromosome 4.
*FIELD* RF
1. Hildebrand, J. D.: Shroom regulates epithelial cell shape via
the apical positioning of an actomyosin network. J. Cell Sci. 118:
5191-5203, 2005.
2. Hildebrand, J. D.; Soriano, P.: Shroom, a PDZ domain-containing
actin-binding protein, is required for neural tube morphogenesis in
mice. Cell 99: 485-497, 1999.
3. Lee, C.; Scherr, H. M.; Wallingford, J. B.: Shroom family proteins
regulate gamma-tubulin distribution and microtubule architecture during
epithelial cell shape change. Development 134: 1431-1441, 2007.
4. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 143-150, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 7/13/2007
Carol A. Bocchini - updated: 7/9/2007
Patricia A. Hartz - updated: 3/22/2004
*FIELD* CD
Stylianos E. Antonarakis: 2/18/2000
*FIELD* ED
mgross: 07/16/2007
terry: 7/13/2007
carol: 7/9/2007
joanna: 4/18/2007
alopez: 4/5/2007
mgross: 3/30/2004
terry: 3/22/2004
mgross: 2/18/2000
*RECORD*
*FIELD* NO
604570
*FIELD* TI
*604570 SHROOM FAMILY MEMBER 3; SHROOM3
;;SHROOM, MOUSE, HOMOLOG OF; SHRM;;
KIAA1481
read more*FIELD* TX
CLONING
Using gene trap mutagenesis, Hildebrand and Soriano (1999) identified a
mutation in mice that caused exencephaly, acrania, facial clefting, and
spina bifida, all of which could be attributed to failed neural tube
closure. This mutation was designated 'shroom' (shrm), because the
neural folds 'mushroom' outward and do not converge at the dorsal
midline. By 5-prime RACE and library screening, the cDNA for the trapped
gene was cloned. Sequence analysis indicated there are at least 2 shrm
transcripts that encode 2 different putative protein products. The
longest predicted transcript, shrmL, encodes a protein of 1,986 amino
acids, while the second transcript, shrmS, encodes a protein of 1,808
amino acids that lacks the N-terminal 177 amino acids of shrmL. Shrm is
a PDZ domain-containing protein related to Xenopus Apx and human APXL
(SHROOM2; 300103).
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned SHRM, which they designated
KIAA1481. The deduced protein shares significant identity with human
APXL. RT-PCR ELISA detected highest expression of SHRM in liver,
followed by kidney, ovary, cerebellum, and spinal cord. Intermediate
expression was found in all other tissues and brain regions examined
except skeletal muscle, where there was little to no expression.
GENE FUNCTION
Hildebrand and Soriano (1999) found that Shrm is involved at several
levels in regulating aspects of cytoarchitecture. First, endogenous shrm
localized to adherens junctions and the cytoskeleton. Second,
ectopically expressed Shrm altered the subcellular distribution of
F-actin. Third, Shrm directly bound F-actin. Finally, cytoskeletal
polarity within the neuroepithelium was perturbed in mutant embryos. In
concert, these observations suggested that Shrm is a critical
determinant of the cellular architecture required for proper
neurulation.
In experiments in Xenopus, Lee et al. (2007) showed that SHROOM3 is
necessary and sufficient to induce a redistribution of the microtubule
regulator gamma-tubulin (see 191135). They found that this change in
gamma-tubulin distribution underlies the assembly of aligned arrays of
microtubules that drive apicobasal cell elongation. They concluded that
Shroom family proteins govern epithelial cell behaviors by coordinating
the assembly of both microtubule and actin cytoskeletons.
Hildebrand (2005) found that Shroom localized to the apical junctional
complex in Madin-Darby canine kidney cells. Overexpression of Shroom
resulted in altered cell morphology with apical constriction and altered
apical cell-cell alignment. Targeting the C-terminal domain of Shroom to
the apical plasma membrane produced similar changes. The neural
epithelia of Schroom-mutant mouse embryos showed a marked reduction in
the apical position of myosin IIB (MYH10; 160776), whereas the positions
of nectin-3 (PVRL3; 607147) and Zo1 (TJP1; 601009) were unaltered.
Hildebrand (2005) concluded that Shroom facilitates the subapical
distribution of nonmuscle myosin IIB, which in turn regulates the tissue
rigidity and cell shape changes required for neural tube closure.
MAPPING
By analyzing a human-rodent hybrid panel, Nagase et al. (2000) mapped
the SHRM gene to chromosome 4.
*FIELD* RF
1. Hildebrand, J. D.: Shroom regulates epithelial cell shape via
the apical positioning of an actomyosin network. J. Cell Sci. 118:
5191-5203, 2005.
2. Hildebrand, J. D.; Soriano, P.: Shroom, a PDZ domain-containing
actin-binding protein, is required for neural tube morphogenesis in
mice. Cell 99: 485-497, 1999.
3. Lee, C.; Scherr, H. M.; Wallingford, J. B.: Shroom family proteins
regulate gamma-tubulin distribution and microtubule architecture during
epithelial cell shape change. Development 134: 1431-1441, 2007.
4. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 143-150, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 7/13/2007
Carol A. Bocchini - updated: 7/9/2007
Patricia A. Hartz - updated: 3/22/2004
*FIELD* CD
Stylianos E. Antonarakis: 2/18/2000
*FIELD* ED
mgross: 07/16/2007
terry: 7/13/2007
carol: 7/9/2007
joanna: 4/18/2007
alopez: 4/5/2007
mgross: 3/30/2004
terry: 3/22/2004
mgross: 2/18/2000