ID A0A2B4SGT2_STYPI Unreviewed; 1436 AA.
AC A0A2B4SGT2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Protein KASH5 {ECO:0000313|EMBL:PFX28050.1};
GN Name=Ccdc155 {ECO:0000313|EMBL:PFX28050.1};
GN ORFNames=AWC38_SpisGene7234 {ECO:0000313|EMBL:PFX28050.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX28050.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX28050.1}.
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DR EMBL; LSMT01000090; PFX28050.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4SGT2; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028168; KASH5_coiled-coil.
DR InterPro; IPR008677; MRVI1.
DR PANTHER; PTHR15352:SF4; LYMPHOID RESTRICTED MEMBRANE PROTEIN; 1.
DR PANTHER; PTHR15352; LYMPHOID-RESTRICTED MEMBRANE PROTEIN, JAW1; 1.
DR Pfam; PF14662; KASH_CCD; 1.
DR Pfam; PF05781; MRVI1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1379..1402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..54
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 797..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..264
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 357..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 538..691
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 881..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1436 AA; 161668 MW; 1B40B7C09232933F CRC64;
MMDTAGPEKD DDPSKISDDA DAVLDNFFYD CDKDNTGRVS VSKLIEYLRN AISSGTEEFA
GSLDDLSLIL DPDGKDMEIG LTSFQEGIKE WISEIRRQSY VNADDECPSP VAVNCMDSPE
ARSYGSPKRF NHVPDIPNAS SDSVEGLGGT SPVKDWDSEL MSTIETLQLN NKRLIEQQSA
IQAQMENTEE GNNLLMAEVE SLRKQLRSAQ LTIEKNKGKE KENAELRQAV ADAMEANQCL
QTKITQLEKE RTLHEGNLKN IDEKSPRCSS PCITSYMVRT RLYDFVSKCD GSKRMQLLET
QAQVELLEEE RKRLVNDLAE QKQYCTDLEE IQGVKNDMIA KESSTNSQMM AGFASQNEAL
KREKGRLEHR VLELEDNLLR LKRSELSAEK NSLVQNGPAA SSTPFVRQSS LQQEILDQET
SETIGLPSPM VGSGLSLNDS LLVDDIDTSL TDLNQSWMSG VSLDSTGTTA SFEKYSLTAR
QLAGEFNLKK EKTLKHLDEL TALNRSVDVR EKREIIREHL AREMDTFAEK TSSLYMKKKA
AEKRTVKLLA IVKKLKEENK EFLEERNEAH QKLRQLALLN DENSAKLLEL EGKHEQDRKT
VTEQNEKLES LEQQLSTVSL DFFKARVEKE SLSRCLENEK RVTTRLEDKV GQLEKNQDEL
ESQQTNLLVQ IKELESELVK ATSQLSMEKR RTSSLEESIQ MSISRHSDEL KDIFEAIPHS
DSELFNRSRQ SPRCSSPCIT SYMVRTRLYD FVSKCDGSKR MQGVGSDYPD QETTKTLQKE
EALETFEDND LFRLRSPSLS SDSLSPQIDR HESDDTCESP SGKFVQLVEN DDRELLTTSC
QTDLKELVST GSQTELLREL QRFERELGVV DKGTCTEEDH FEYEKQRRRR SGIIESPGPE
VRTLGTTPKS SEETPTKITG GDSSSGKATL SVEKDKTATN LWRKKLSVAF KIPEEFDYES
ATSAALENSV GGNNFVDGVS LRVRPALNDK EIEKQFKTLV LAFQTDHDTL NRRLEVQARA
REIAESNMNK ELQSMSNSLK DMLSLLKTHL EIIKKSSQRI ITQTEQHGCV KQEARMSSGV
EVMICHAENL TRHLERVRED LNELRMKERL VADESASPGT LANGPTRLGI DSQTVSSPSS
PLPHQEARMS SGVEVMICHA ENLTRHLERV REDLNDLRMK ERLVADESAS PGTLANGPTR
LGIDSQTVSS PSSPLPHQSE GGGDGTKQNS LLNFVMAFHT TSMRAKEALR SFRRRTEASR
QEREASASPV RQTEEPSGKK MDSSLTESMP EAESSGTPVV VVSDSEGEND NINTELREGT
QDEHEDEMVT VHLPAESEGN DQIKDASENE SESDVLDSEV NSFQETSKRP SVCWRFLSAA
FRFTTFVVIF LLIIFIGVTI FVKTDIVVIE RDFVMSRLRK LLDPFIEVVY HEVPPQ
//
