SHRM1_XENLA
ID SHRM1_XENLA Reviewed; 1420 AA.
AC Q01613;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein Shroom1;
DE AltName: Full=APX;
DE AltName: Full=Apical protein;
GN Name=shroom1; Synonyms=apx;
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], AND FUNCTION.
RC TISSUE=Ovary;
RX PubMed=1334959; DOI=10.1083/jcb.119.6.1497;
RA Staub O., Verrey F., Kleyman T.R., Benos D.J., Rossier B.C.,
RA Kraehenbuhl J.-P.;
RT "Primary structure of an apical protein from Xenopus laevis that
RT participates in amiloride-sensitive sodium channel activity.";
RL J. Cell Biol. 119:1497-1506(1992).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SCNN1A.
RX PubMed=10438504; DOI=10.1074/jbc.274.33.23286;
RA Zuckerman J.B., Chen X., Jacobs J.D., Hu B., Kleyman T.R., Smith P.R.;
RT "Association of the epithelial sodium channel with Apx and alpha-spectrin
RT in A6 renal epithelial cells.";
RL J. Biol. Chem. 274:23286-23295(1999).
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).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Induces gamma-tubulin accumulation at cell-cell junctions and
CC may direct the assembly of robust microtubule arrays during cell
CC elongation. May regulate the surface expression of amiloride-sensitive
CC sodium channel. {ECO:0000269|PubMed:10438504,
CC ECO:0000269|PubMed:1334959, ECO:0000269|PubMed:17329357}.
CC -!- SUBUNIT: Interacts with F-actin (By similarity). Interacts with scnn1a.
CC {ECO:0000250, ECO:0000269|PubMed:10438504}.
CC -!- SUBCELLULAR LOCATION: Apicolateral cell membrane
CC {ECO:0000269|PubMed:10438504}. Apical cell membrane
CC {ECO:0000269|PubMed:10438504}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10438504}.
CC -!- TISSUE SPECIFICITY: Kidney, proximal intestine, oocytes, and to a
CC lesser extent in the distal intestine, stomach and eye. Epithelial
CC cells of the cement gland. {ECO:0000269|PubMed:17329357}.
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; Z14997; CAA78718.1; -; mRNA.
DR PIR; A44361; A44361.
DR RefSeq; NP_001084156.1; NM_001090687.1.
DR AlphaFoldDB; Q01613; -.
DR SMR; Q01613; -.
DR GeneID; 399339; -.
DR KEGG; xla:399339; -.
DR CTD; 399339; -.
DR Xenbase; XB-GENE-6254041; shroom1.L.
DR OrthoDB; 29607at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 399339; Expressed in pancreas and 19 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 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; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW Microtubule; Reference proteome.
FT CHAIN 1..1420
FT /note="Protein Shroom1"
FT /id="PRO_0000064651"
FT DOMAIN 518..620
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1150..1419
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 225..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1420 AA; 159468 MW; 0DD8B5C11413FFBC CRC64;
MSAFGNTIER WNIKSTGVIA GLGHSERISP VRSMTTLVDS AYSSFSGSSY VPEYQNSFQH
DGCHYNDEQL SYMDSEYVRA IYNPSLLDKD GVYNDIVSEH GSSKVALSGR SSSSLCSDNT
TSVHRTSPAK LDNYVTNLDS EKNIYGDPIN MKHKQNRPNH KAYGLQRNSP TGINSLQEKE
NQLYNPSNFM EIKDNYFGRS LDVLQADGDI MTQDSYTQNA LYFPQNQPDQ YRNTQYPGAN
RMSKEQFKVN DVQKSNEENT ERDGPYLTKD GQFVQGQYAS DVRTSFKNIR RSLKKSASGK
IVAHDSQGSC WIMKPGKDTP SFNSEGTITD MDYDNREQWD IRKSRLSTRA SQSLYYESNE
DVSGPPLKAM NSKNEVDQTL SFQKDATVKS IPLLSQQLQQ EKCKSHPLSD LNCEKITKAS
TPMLYHLAGG RHSAFIAPVH NTNPAQQEKL KLESKTLERM NNISVLQLSE PRPDNHKLPK
NKSLTQLADL HDSVEGGNSG NLNSSAEESL MNDYIEKLKV AQKKVLRETS FKRKDLQMSL
PCRFKLNPPK RPTIDHFRSY SSSSANEESA YLQTKNSADS SYKKDDTEKV AVTRIGGRKR
ITKEQKKLCY SEPEKLDHLG IQKSNFAWKE EPTFANRREM SDSDISANRI KYLESKERTN
SSSNLSKTEL KQIQHNALVQ YMERKTNQRP NSNPQVQMER TSLGLPNYNE WSIYSSETSS
SDASQKYLRR RSAGASSSYD ATVTWNDRFG KTSPLGRSAA EKTAGVQRKT FSDQRTLDGS
QEHLEGSSPS LSQKTSKSTH NEQVSYVNME FLPSSHSKNH MYNDRLTVPG DGTSAESGRM
FVSKSRGKSM EEIGTTDIVK LAELSHSSDQ LYHIKGPVIS SRLENTRTTA ASHQDRLLAS
TQIETGNLPR QTHQESVVGP CRSDLANLGQ EAHSWPLRAS DVSPGTDNPC SSSPSAEVQP
GAPEPLHCLQ TEDEVFTPAS TARNEEPNST AFSYLLSTGK PVSQGEATAL SFTFLPEQDR
LEHPIVSETT PSSESDENVS DAAAEKETTT TQLPETSNVN KPLGFTVDNQ EVEGDGEPMQ
PEFIDSSKQL ELSSLPSSQV NIMQTAEPYL GDKNIGNEQK TEDLEQKSKN PEEDDLPKVK
LKSPEDEILE ELVKEIVAKD KSLLNCLQPV SVRESAMDLM KSLFPMDVTA AEKSRTRGLL
GKDKGETLKK NNSDLESSSK LPSKITGMLQ KRPDGESLDD ITLKKMELLS KIGSKLEDLC
EQREFLLSDI SKNTTNGNNM QTMVKELCKP NEFERYMMFI GDLEKVVSLL FSLSTRLTRV
ENSLSKVDEN TDAEEMQSLK ERHNLLSSQR EDAKDLKANL DRREQVVTGI LVKYLNEEQL
QDYKHFVRLK TSLLIEQKNL EEKIKVYEEQ FESIHNSLPP
