SHRM2_XENTR
ID SHRM2_XENTR Reviewed; 1726 AA.
AC Q09JY9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein Shroom2;
DE AltName: Full=Protein Apxl;
GN Name=shroom2; Synonyms=apxl;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16987870; DOI=10.1242/dev.02563;
RA Fairbank P.D., Lee C., Ellis A., Hildebrand J.D., Gross J.M.,
RA Wallingford J.B.;
RT "Shroom2 (APXL) regulates melanosome biogenesis and localization in the
RT retinal pigment epithelium.";
RL Development 133:4109-4118(2006).
CC -!- FUNCTION: May be involved in endothelial cell morphology changes during
CC cell spreading. Required for eye pigmentation. In the retinal pigment
CC epithelium, regulates the biogenesis of melanosomes and promotes their
CC association with the apical cell surface by inducing gamma-tubulin
CC redistribution. {ECO:0000269|PubMed:16987870}.
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 -!- DEVELOPMENTAL STAGE: At stage 25, expressed throughout the eye field.
CC At stage 40, expression becomes restricted to the retinal pigment
CC epithelium. {ECO:0000269|PubMed:16987870}.
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; DQ886532; ABI63573.1; -; mRNA.
DR RefSeq; NP_001072178.1; NM_001078710.1.
DR AlphaFoldDB; Q09JY9; -.
DR SMR; Q09JY9; -.
DR STRING; 8364.ENSXETP00000060716; -.
DR PaxDb; Q09JY9; -.
DR GeneID; 779568; -.
DR KEGG; xtr:779568; -.
DR CTD; 357; -.
DR Xenbase; XB-GENE-982291; shroom2.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR InParanoid; Q09JY9; -.
DR OrthoDB; 29607at2759; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
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; IMP:HGNC-UCL.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; IDA:HGNC-UCL.
DR GO; GO:0007420; P:brain development; IEP:HGNC-UCL.
DR GO; GO:0043010; P:camera-type eye development; IEP:HGNC-UCL.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:HGNC-UCL.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0043482; P:cellular pigment accumulation; IMP:HGNC-UCL.
DR GO; GO:0043583; P:ear development; IEP:HGNC-UCL.
DR GO; GO:0032401; P:establishment of melanosome localization; IMP:HGNC-UCL.
DR GO; GO:0008057; P:eye pigment granule organization; IMP:HGNC-UCL.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:HGNC-UCL.
DR GO; GO:0032438; P:melanosome organization; IMP:HGNC-UCL.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR027686; Shroom2.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR PANTHER; PTHR15012:SF8; PTHR15012:SF8; 1.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 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 2: Evidence at transcript level;
KW Actin-binding; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Developmental protein; Membrane; Microtubule; Reference proteome;
KW Tight junction.
FT CHAIN 1..1726
FT /note="Protein Shroom2"
FT /id="PRO_0000286065"
FT DOMAIN 79..159
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 788..877
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1427..1721
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 294..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1726 AA; 195259 MW; 932DE44A9AE58A23 CRC64;
MLVLGCLQCF TSAWGFASRR ICHSSSATPG QHSVGLGHGY QHGAQSWAER FLLRYKGLLW
FVGSRAHSGG EETNGKLQAG GCYSYWRGSL GIYFERGKEH GEPLIITKVE DGNKAADILM
AGDEIVNIND QQLLGYRQEA ICLVKGSHKI LKMIVKRRND ISYRPHSWHS NKLIESAMDT
VTPQMSNASP FWNARYRSSS SSHDLSNPWD QTSLQRNSGH FSSMGSMDSI DQTYQFGRLS
SAKSNNSIDY VGSQNKRDSA YGSFSASFST PDHTLSKTAS ASTENILYKN NEWDNTKLGY
GKTSPSMNEV RRSADRQVLQ STSINETSKI QRTEDNTEPR YSGRSNFGPV WNIPDKKKTA
SPPPPPPPQR SDSYAVTKIH EKPTNLMHLD ASSTQHFNVA NRSQAKPDWS LEISEQQRPI
RAHDRTVADT RRTSNSSYHA GLNADQGLSP YKDKYPSNLP NVSRIQASLS TNDVRFAQPA
YNYHHQRQYS DESTLFQSTR TSAQHKSQQQ PMKYESSVNQ VPSDLTYVYH PHQFRAPATS
AGFSSGKQNV ENNGQNHFHV VSIKHPQGNT THHQFKEEEN YAPEVNSGRK SVQPENTVIS
IEIPAYSLPQ ESFEPSQINC EKNYLKISEK KDNYLGNNEQ IINKTTGYSE EKCNDRFSQL
DHSEKGSYRS SQDYSWRKEE NKITPLVTPM LHSLAQEGRN RSESFPDTGN EKLSFPDAGK
QSRRSDRFAT TLRNEIQQRR ARLQKSKSTA ALTESNETET SDNWKQDSLE SMSPTSEGSF
SSTYRSHLQE AQARVLRATS FKRRDLDTGI SDHLSLFQDR NMQISSFSGL SLDPVQPKKN
TAVNSSQNVS RIGARKRFTT QQKLMSYSEP EKINEVGVED QYNFRTENST KRTVGSFADR
WKFFEETSKC AQPKVPPKVV SSSQSEETSE IAINRDYAKS SEGQESKRAL AVSGQNPADE
NGFPDKVTTE RRQRLGTFAE YEASWKEQKT QLERKNSGRC HSADNILDAD LEQNPKAQYI
HERSKSSPTT DFYAQAAAVE SKQQSESVRR DTENSNSTHC RSSTGDSPTR TVEAGDQCGA
TNEQEVLTCN TKWKPHDKSF PIPETSNESQ QSRARSGTLP NDYRFAHENV NQGNRDISFS
AVPISEACPD FSNADSDQLQ DHPSVFKKRS AAPQRPPPPK LENKYWRQNG SSSSLATSSE
SLLTAQARRA QSYSPSSQDT FPPQSLQKQS PSTYPDKNPS IHIYDYQLSV PPENDRYHLE
KKYFESELSS KSHLQIPGME PSRSPSPQFA PQKLTDKPPL LVPEENLSRI ERVIDNTTVK
MVPIKIVHSE THAEKESRHN LLSAIEPTAL PTGLAKDQLK TLSTSEQSYS RFCAYTRQES
REEEESRVTD LYSCQRNAED DNENDVSSLA PSNAKSKDAI YADLKSEELV REIVDKDKSL
ADILDPNAKM RTTMDLMEGI FPKDEHLLEE AQQRRKHLPK IPSPRSTDDK KDEQNVPSAV
SLTTSSTYYS TSAAKAELLI KMKDMQEQQH IAENSEDELG QNLSEKKQEL IDSISKKLQV
LRDAKETLLE DVQCNNALGE EVEIIVKEVC KPNEFDKFRM FIGDLEKIVN LLLSLSGRLA
RVENALNNLD ETVSPEERKT LLEKRKLLTR QHEDAKELKE NLDRRERTVY EILANYLNEE
NLADYEHFVK MKSALILEQR ELEDKIKLRE SQLKCLTDSL PLDRIK
