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Database: UniProt
Entry: A0A1S3WMG6_ERIEU
LinkDB: A0A1S3WMG6_ERIEU
Original site: A0A1S3WMG6_ERIEU 
ID   A0A1S3WMG6_ERIEU        Unreviewed;      1411 AA.
AC   A0A1S3WMG6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=LIM domain only protein 7 isoform X2 {ECO:0000313|RefSeq:XP_016047545.1};
GN   Name=LMO7 {ECO:0000313|RefSeq:XP_016047545.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016047545.1};
RN   [1] {ECO:0000313|RefSeq:XP_016047545.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_016047545.1; XM_016192059.1.
DR   CTD; 4008; -.
DR   OrthoDB; 6462at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR   CDD; cd08368; LIM; 1.
DR   CDD; cd00136; PDZ; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   InterPro; IPR031865; DUF4757.
DR   InterPro; IPR029978; LMO-7.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR46767; LIM DOMAIN ONLY PROTEIN 7; 1.
DR   PANTHER; PTHR46767:SF1; LIM DOMAIN ONLY PROTEIN 7; 1.
DR   Pfam; PF15949; DUF4757; 2.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          760..841
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1340..1406
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          26..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1010..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1240..1334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          945..995
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        489..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1133..1160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1247..1334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1411 AA;  161618 MW;  D9040529F18E6DDB CRC64;
     MQDYNKDDMS YRRISAIEPK SALPFNRFLP NKSRQPSYVP APLRKKKPDR NEDNRRSWAS
     PASSEADGTF SRLDVLSSNE RRTWDTNMEN WSAVQATSHS SRYLEEKEKT NMPNIVKDDL
     YVRKLSPVMP NPGNAFNQFL PKCWIPEDVN CKRIKRETYK PWYKEFQGFS QFLLLHALQT
     YSDDILSSET NTRIDPTSGP RLITRRKNRF YTPGYRRDDH EISSVNPDLE NDDFFVRKTG
     AFHANPCVLQ AFEDFRRFSE QDDPVERDII LQCREGEIVL PDLEKDDMII RRIPAQKKEV
     PLSGAPDRYQ PVPFPEPWTL PPEIQAKFLC VLERTCPTRE KSSNSCRVLV PSHRQKKDDM
     LTRKIQSWKL GTAVSPISFT PGPCSEADLK KWEAIREASR LRHKKRLMVE RLFQKIYGEN
     GSKSMSDVTA EDVQNMRQLR YEEMQKIKSQ LKEQDQKWQD DLAKWKDRRK SYTSDLQKKK
     EEREEIEKLA LEKSEKNSKT LKEMQQDRES RNQMTAITSR RRIYSHDDVL NEEIFSPPVT
     MSETHDQSER AEEMGTTYPT EIPKHDSTTL VKREDSVAAE IPLPSNSTAE GQRPASLSSQ
     LLLSTQMEST RVSTSLPRSY QKTDTARLTS VVTPRPFGSH SRGISSLPRS YTMDAAWKYN
     GDVEGVKRTQ NTCVNTSVQK PDPSQLTSSL PSERETVAEE VTRVPSPIAS LSPSSQDQSV
     TSQVTLSSTS GLDLMSESGV GRSSPQREVS KSQDQFSDMR ISINQKPGNS IVLGFTVKWD
     FSGISIASVE AGSPAEFSQL QVDDEIIAIN NIKFSRKDTK EWEEAMANAQ ETGNLVMDIR
     RYGKSGSPET KWIDATSGIY NSDKSSNLSI TTDFSESLQD SNVESKEING IRDERNTFES
     KASEPISLKN LKRRSQFFEQ GSSDSMVPDL PVPTISAPSR WAWDQEEERK RQEKWQKEQD
     RLLQEKYQRE QEKLREEWQI AMQEAERENS KYLNEELMVL TSNNIALTPR EPEATSWETT
     WGVESKSSDK EGTRAGEEER RPQQEDSLTE DQNKKLQEHL SLEKERKLKE EQQYQEEQEQ
     KQRQYQEERE LRRRQAEAEA EERARLGEEL KHQAERERET SVKIYQYRRP VDSYDVSGRE
     EESSGLLPSD RNKSRSTTEL DDYSSSKNGN NRYLDRIGNT SSLQKSSKKE QAPSGAELER
     QQILQEMRKR TSLHNDNSWI RQRSSSVNKE PICLPGIMRR GESLDNLDSP RSNSRRQSPW
     HNQSTGVYAS SSVQDFSRPP PQLLSTSNRA YMRNPSSGVP PPSSGSGKTP SAPSPPSRSQ
     SPSTTQSGSQ LRNRSVSGKR VCSYCNNILG KGAAMIIESL GLCYHLHCFK CVACERDLGG
     SASGAEVRIR NNQLYCNDCY LRFKSGRPTA M
//
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