ID A0A3B4E420_PYGNA Unreviewed; 1639 AA.
AC A0A3B4E420;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Capping protein regulator and myosin 1 linker 2 {ECO:0000313|Ensembl:ENSPNAP00000030438.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000030438.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000030438.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CARMIL family.
CC {ECO:0000256|ARBA:ARBA00007298}.
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DR Ensembl; ENSPNAT00000018493.1; ENSPNAP00000030438.1; ENSPNAG00000017448.1.
DR GeneTree; ENSGT00940000155112; -.
DR Proteomes; UP000261440; Unplaced.
DR Gene3D; 6.10.140.1850; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR031943; CARMIL_C.
DR InterPro; IPR041245; CARMIL_PH.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR24112:SF32; CAPPING PROTEIN, ARP2_3 AND MYOSIN-I LINKER PROTEIN 2; 1.
DR PANTHER; PTHR24112; LEUCINE-RICH REPEAT, ISOFORM F-RELATED; 1.
DR Pfam; PF17888; Carm_PH; 1.
DR Pfam; PF16000; CARMIL_C; 1.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00368; LRR_RI; 4.
DR SUPFAM; SSF52047; RNI-like; 2.
PE 3: Inferred from homology;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614}.
FT DOMAIN 24..117
FT /note="CARMIL pleckstrin homology"
FT /evidence="ECO:0000259|Pfam:PF17888"
FT DOMAIN 779..1146
FT /note="CARMIL C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16000"
FT REGION 912..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1639 AA; 180004 MW; 51DD35D63234C0DD CRC64;
MASQAEVPFC LKDAIIQLLR PQKVRFMRLV QLNQSRDRSE GRVLVMTQWR AHMFHSKQPV
KVESSFSYLE IYAIIIESLE QVIIETDRQI YSLSLMSMED LEAMVSHVTA SLKKVFPDSS
PGKLLKKIPP ELQDRLCSLS SRVEEQLNGA HGPCGGFSDT YAALCDFNEF QCREEVQWDV
DNIYHVQNCR EFNLLDFSYL DSRDLALAVG ALSFNQWFTK ICSKDFKLTL DVQEQVIYLI
NRSTALQELC LEAGGLKADF VVKLACALRE QPASALHVIN LSANSIEDKG AMSLSQSLAR
LPNGLSQLYL SKVSLSSKGL GSIANMLYQT KSLSNLLTHL DLSGNTGCLA TEDAMNLFKF
LSAQNIVSHL DLSSTDCPLD ALFVSLSTGC YTTLSYLSLS RNPFSHRKVR EVTRSVRDFF
TKSMKLKYVG LAGTKLPPDA LRLLLQGLAT NSYLSELELD ISSCELRSSG AQVIQEHIFE
TKAIGSLDLS DNGFEHDMVT LVLSIGRSHS IRHLALGRNF AMKSRALTDV LHRIVQLIQE
EECPLESLSV SDSKLKTGTT ILINSLGSNS GLSKIDISGN CIGDTGAKML AKALMINTKL
KTLVWDRNSV SATGFMDVAN ALERNTTLLH MSIPMSDMAQ SYRSNPEKTE EAMQKIQTCL
RRNSERIFTT PDEMLNLQQG LKTSRSEQLV QHVCQKLQET MRPLSCYNIQ EVQSDILSAE
EALQHARIAI TSLPRLYELG RSPPAGSTVQ HILDDAARAI TSELTEEIQE QAQMMLQFAQ
AVCPRVVQRT SVSEQLANRV ATKTRQATHF IHSTVQQAEN SIREKLSELK VSVSVSLVES
IIEEVLQDLS VAQQKLDKHL KEYSQPFSSK TNVPQLRVVE NEFPTDEYVP VMWRNSFCTR
SIRPAPSVKS LLEGEGEQQA RASAHSQQEV EERERARARE RERGGGGAQG SRLTAEERRR
SLTFSSSLVT GLSVMTAVGG ARTLGPAQPG MGAGPVGSGC GAAAGSNSTQ PRRPEPASTQ
PPMDLPIEGQ TLRHYTRSRP RPNRRNRQPP SKPQEQAAES ENEANENMGR VDEGVEEFFT
KKIIPDDPLK HQREEPLNKA QPAESTCVTT TPPTTTTTTT PTPSTAPSKN IKKKFGDFFA
FKKVRAGRGA KGEGAPEGKV KKTSIADLIR PLREAARAEK EREKEREREK EREREKGREK
EKEKAEEDSI VKAPTTTPTI TDSALTAPAV DDKMAPRSPS PLLMPILAPS AASASTPIPP
ASSPAKTEEA PALSPAAPTS PTKTPSPVAA VSPSEREKSR TPDGERRPKP TRRSLREGKS
QSLILLTGLE PEHDAAVIQA KKHASESSSS FEQRIHGLLH RIGVTKTPPS DSKTSQSKDE
ELRKANSEGA ILDSKPEPPP TYMKPRTMST SSDTRRPGRG GNVESLRADR PPLPERPIGP
LPPKPALKPT LIPPSETPAA SRTITPAPRQ PSPSPDAQPL AVETGPSTQA QTKEPPTPSP
RKETPPAPSP RRVLSTDVRE RAERAQSVTE ELKAALPRLQ RSPVRKRVNL GELEPCSEDL
PEGEEAKTEG RGDGRGQAGE TGSTTVSESP PEASVVGPGE DRSRQELGEM VSEQDQQHTA
QGETSDQRTE TPSPETNMD
//
