ID A0A2Y9NN14_DELLE Unreviewed; 1267 AA.
AC A0A2Y9NN14;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=LIM domain only protein 7 isoform X10 {ECO:0000313|RefSeq:XP_022432732.1};
GN Name=LMO7 {ECO:0000313|RefSeq:XP_022432732.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022432732.1};
RN [1] {ECO:0000313|RefSeq:XP_022432732.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022432732.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_022432732.1; XM_022577024.2.
DR AlphaFoldDB; A0A2Y9NN14; -.
DR Proteomes; UP000248483; 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; cd21277; CH_LMO7; 1.
DR CDD; cd08368; LIM; 1.
DR CDD; cd00136; PDZ; 1.
DR Gene3D; 2.30.42.10; -; 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; IPR029978; LMO-7.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR003096; SM22_calponin.
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; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
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:UP000248483};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 22..139
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 664..745
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1196..1262
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 268..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 143299 MW; CAACB6BF0C52364E CRC64;
MSLSPPLPLV LEVMEEAEAD CALAFAEAQR WVEAVTEKNF ETKDFRASLE NGVLLCDLIN
KLKPGVIKKI NRLSTPIAGL DNINVFLKAC EQIGLKEAQL FHPGDLQDLS NRVTVKQEET
DRRVKNVLIT LYWLGRKAQS NPYYNGPYLN LKAFENLLGQ ALTKALEESS FLKRSGRDSG
YGDIWCAERG EFLAPPGNYK REDSFESLDS LGSRSFTSCS SDITLRGARE GCESDTDSEF
TFKMQDHNKD DMSYRRISAV EPKSALPFNR FLPNKGRQPS YVPAPLRKKK LDKNEDNRRT
WASPVCIEAD RTFPRLFQKI YGENGSKSMS DVSAEDAQNL RQLRYEEMQK IKSQLKEQDQ
KWQDDLAKWK DRRKSYTSDL QKKKEEREEI EKQSLEKPER RSKTFNEMLQ DRESPNHMST
VTSRRKLYSS DDGVSEEKLP PMLTMSEVSS QSERVEEKGT TYPTEIPKQD STAFAKREAT
ITAEIQLPSK SPVEEQRPAS LSSQHSRQME STRVSATLPR SYQKTDAARL TSVVTPRPFG
SQSRGISSLP RSYTMDDSWK YNGDVEGIKR TQSSSVSISV QRPDTSQFAS RSSSEREAAA
PRESVMRLLS PTPTFSSPSQ GQAATSKDTL SSTSSPDLTP ELGEGKSSPQ TEVSRSQDQF
SDMRISINQT PGNSLDFGFT VKWDFSRIFV ASVEPGSPAE FSQLQVDDEI IAINNTKFSY
KDTKEWEETM ANAQETGNLV MDIRRYGKSG SPETKWIDAT SGIYSSDKSS NLSITADFSE
SLQNSNTESK EINGIRDESN TFESKASEPI SLKNLKRRSQ FFEQGSSDSV VPDLPVPTIS
APSRWTWDQE GERKRQERWQ KEQDRLLQEK YQREQEKLRE EWQRAKQEAE RENSKYLNEE
LMVLNSNSIS LTTREPAVAT RGEESKAPDS EGTPAEEETR QQQQQEKDQE QKQRQAEAEA
EAEADEQKRR AERERETSIQ IYQYRRPVDS YDIPKREEES SGLLPSDRNK SRSTTELDDY
PTNKNGSNRY LDRTGSSSSS QKSSKKEQVP SGAELERQQI LQEMRKRTSL YDDNSWIRQR
SSSVNKEPIC LPGIMRRGES LDNLDSPRAS SWRQSPWLNQ PSGVYATSSV QDFSRPPPQL
LSTSNRAYMR NPSSGVPPPS AGSGKTTTPS PILRSHSPAV PQPGCQPRNR SVSGKRVCSY
CHNILGKGAA MIIESLGLCY HLHCFKCVAC DRDLGVSSSG AEVRIRNNQL YCNDCYLRLK
SGRPTAM
//
