ID A0A2I2ZRJ0_GORGO Unreviewed; 1104 AA.
AC A0A2I2ZRJ0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=LIM and calponin homology domains 1 {ECO:0000313|Ensembl:ENSGGOP00000049864.1};
GN Name=LIMCH1 {ECO:0000313|Ensembl:ENSGGOP00000049864.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000049864.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000049864.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000049864.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000049864.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; CABD030028100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030028109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2ZRJ0; -.
DR Ensembl; ENSGGOT00000059027.1; ENSGGOP00000049864.1; ENSGGOG00000003779.3.
DR GeneTree; ENSGT00950000183159; -.
DR Proteomes; UP000001519; Chromosome 4.
DR Bgee; ENSGGOG00000003779; Expressed in heart and 6 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08368; LIM; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR15551:SF3; LIM AND CALPONIN HOMOLOGY DOMAINS-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR15551; LIM DOMAIN ONLY 7; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 1.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 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:UP000001519};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 42..146
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1032..1098
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 206..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 375..460
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 803..844
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 206..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 124306 MW; 1576AF19E4518586 CRC64;
MESRSVAQAG VQWCDLGSLQ APPPGFTPFS CLSLPSSWDY RHPKTYVLFS FLQQVTGRSF
GDKDFRTGLE NGILLCELLN AIKPGLVKKI NRLPTPIAGL DNIILFLRGC KELGLKESQL
FDPSDLQDTS NRVTVKSLDY SRKLKNVLVT IYWLGKAANS CTSYSGTTLN LKEFEGLLAQ
MRKETDDIES PKRSIRDSGY IDCWDSERSD SLSPPRHGRD DSFDSLDSFG SRSRQTPSPD
VVLRGSSDGR GSDSESDLPH RKLPDVKKDD MSARRTSHGE PKSAVPFNQY LPNKSNQTAY
VPAPLRKKKA EREEYRKSWS TATSPLGGER PFRYGPRTPV SDDAESTSMF DMRCEEEAAV
QPHSRARQEQ LQLINNQLRE EDDKWQDDLA RWKSRRRSVS QDLIKKEEER KKMEKLLAGE
DGTSERRKSI KTYREIVQEK ERRERELHEA YKNARSQEEA EGILQQYIER FTISEAVLER
LEMPKILERS HSTEPNLSSF LNDPNPMKYL RQQSLPPPKF TATVETTIAR ASVLDTSMSA
GSGSPSKTVT PKAVPMLTPK PYSQPKNSQD VLKTFKVDGK VSVNGETVHR EEEKERECPT
VAPAHSLTKS QMFEGVARVH GSPLELKQDN GSIEINIKKP NSVPQELAAT TEKTEPNSQE
DKNDGGKPRK GNIELASSEP QHFTTTVTRC SPTVAFVEFP SSPQLKNDVS EEKDQKKPEN
EMSGKVELVL SQKVVKPKSP EPEATLTFPF LDKMPEANQL HLPNLNSQVD SPSSEKSPVT
TPQFKFWAWD PEEERRRQEK WQQEQERLLQ ERYQKEQDKL KEEWEKAQKE VEEEERRYYE
EERKIIEDTV VPFTVSSSSA DQLSTSSSMT EGSGTMNKID LGNCQDEKQD RRWKKSFQGD
DSDLLLKTRE SDRLEEKGSL TEGALAHSGN PVSKGVHEDH QLDTEAGAPH CGTNPQLAQD
PSQNQQTSNP THSSEDVKPK TLPLDKSINH QIESPSERRK KSPREHFQAG PFSPCSPTPP
GQSPNRSISG KKLCSSCGLP LGKGAAMIIE TLNLYFHIQC FRCGICKGQL GNAVSGTDVR
IRNGLLNCND CYMRSRSAGQ PTTL
//