ID A0A287AMS3_PIG Unreviewed; 1628 AA.
AC A0A287AMS3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 3.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=LIM and calponin homology domains 1 {ECO:0000313|Ensembl:ENSSSCP00000045345.3};
GN Name=LIMCH1 {ECO:0000313|Ensembl:ENSSSCP00000045345.3,
GN ECO:0000313|VGNC:VGNC:89724};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000045345.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000045345.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000045345.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000045345.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 9823.ENSSSCP00000045345; -.
DR PaxDb; 9823-ENSSSCP00000026940; -.
DR Ensembl; ENSSSCT00000039961.3; ENSSSCP00000045345.3; ENSSSCG00000008799.5.
DR VGNC; VGNC:89724; LIMCH1.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00950000183159; -.
DR InParanoid; A0A287AMS3; -.
DR ChiTaRS; LIMCH1; pig.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000008799; Expressed in skeletal muscle tissue and 42 other cell types or tissues.
DR ExpressionAtlas; A0A287AMS3; baseline and differential.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032034; F:myosin II head/neck binding; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IBA:GO_Central.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IBA:GO_Central.
DR CDD; cd21278; CH_LIMCH1; 1.
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; IPR001997; Calponin/LIMCH1.
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; 2.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00889; CALPONIN.
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 1: Evidence at protein level;
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287AMS3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 21..125
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1556..1622
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 185..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1628 AA; 182207 MW; 287CB0100EF02C78 CRC64;
MACPALGLEA LQPLQPEPPP EPAFSEAQKW IEQVTGRSFG DKDFRTGLEN GILLCELLNA
IKPGLVKKIN RLPTPIAGLD NIILFLRGCK ELGLKESQLF DPSDLQDTSN RVTVKSLDYS
RKLKNVLVTI YWLGKAANSS ASYSGTTLDL KEFEGLLAQM RKETDDIESP KRSIRDSGYI
DCWDSERSDS LSPPRHGRDD SFDSLDSFGS RSRQTPSPDV VLRGSSDGRG SDSESDLPHR
KLPDVKKDDM SARRTSHGEP KSAVPFNQYL PNKSNQTAYV PAPLRKKKAE REEYRKSWST
ATSPLGGERP FSYPETIEEE GSEVGSSCEE DPVGQMDPRG KPPDGGLELS PSRGKEQPPP
EGATVAAAPK AEEKDAVEIQ KRRRLEQAGI KVMPAAQRFA SQKQLSDERE AVRDIILRRE
NPFLVHQSGK DPESEDEVAC RLPDLEKDDF AARRARMNQT KPMVPLNQLL YGPPEKRAEK
SDGSKQLSKG ISEKKNLEHK RNQGHTEEVK PRVTCIVRAQ EHEPAGEGLR KVPDLYKDDL
AQRRIQGRLG PHREAPSFVT VSNITEADLE TWERLKVSGK TRDGDVEHTC APEPSPEIKA
ETAIRDDFAS RKTRAYEKAS GPRQKFVHFG PVTEIDQQTW RRLSIGKAGP REEAEEVISH
GSTIQTDSVS PASPATSSLK EEPVLSPQND HRIVTSSVDD CPTRVSRLAP VPEPQEEPSC
SLGECPRRTE EVTCKQLPQG SKEENEGAVQ RDSEKAPKAE RSAEESGQPL SCPLTSKWEA
LEKEEKLEKM TAPAWSGSGL KGQRKLSDSQ KDDMTARRTG MFLRHTGSNP NQFLPVPFAK
QHSMEDSAKG PPIKDKRYGP RTPVSDDAES TSMFDMRCEE EAAVQPHSRA RQEQLQLINN
QLREEDDKWQ DDLARWKSRR RSASQDLIKK EEERKKMEKL LAGEDGTRER RKSIKTYREI
VQEKERRERE LHEAYKNARS QEEAEGILQQ YIERFTISEA VLERLEMPKI LERSHSAEPN
SSSFLDDPNP MKYLRQQSLP PPKFTATVET TITRTSVPDA SMSAGSGSPS KTVTPKAVPM
LTPKPYSQPK NSQEVLKTFK VDGKVSMNGE TVHGDEEKER ECPPGAHTPS LTKSQMFEGV
ARVHGSPVEL KQDNNSIEIN IKKPSSLPQE LPATIEETDA NRQEDESDGE KREKGNTDIV
SPEPQHFTTT VTRSSPTVAF VELSSSPQLK NEVPEEKEQK KLENEMSGKV ELVLSQKVVK
PKSPEPEATL TFPFLDKMPE TNQLHLPNLN SQVDSPSSEK SPVTTPFKFW AWDPEEERRR
QEKWQQEQER LLQERYQKEQ DKLKEEWEKA QKEVEEEERR YYEEERKIIE DTVVPFTISS
SSADQLSTSS SMTEGSGTVT KMDLENCQEE EQETRQKKPL QGDNSDLLLK TGDGDPLEEK
GSLTQGVLTH SENPASKGIY QDHQLDAEAG ASHCGMNPQP AQDPSQNQQV SNPPMHILED
VKPKTLPLDK SINHQIESPS ERRKKSPREN FQAGHLSPCS PTPPGQSPNR SISGKKLCSS
CGLPLGKGAA MIIETLSLYF HIQCFRCGIC KGQLGDAVSG TDVRIRNGLL NCNDCYMRSR
SAGQPTTL
//
