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Database: UniProt
Entry: A0A369SLI5_9METZ
LinkDB: A0A369SLI5_9METZ
Original site: A0A369SLI5_9METZ 
ID   A0A369SLI5_9METZ        Unreviewed;      2436 AA.
AC   A0A369SLI5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Spectrin alpha chain, non-erythrocytic 1 {ECO:0000313|EMBL:RDD47344.1};
GN   ORFNames=TrispH2_000403 {ECO:0000313|EMBL:RDD47344.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD47344.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD47344.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD47344.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD47344.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826}.
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:RDD47344.1}.
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DR   EMBL; NOWV01000003; RDD47344.1; -; Genomic_DNA.
DR   STRING; 287889.A0A369SLI5; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd11856; SH3_p47phox_like; 1.
DR   CDD; cd00176; SPEC; 12.
DR   Gene3D; 1.20.58.60; -; 18.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 20.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 20.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 17.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          969..1028
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          2286..2321
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          2329..2364
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   COILED          300..327
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          391..457
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1133..1167
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1239..1266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1588..1629
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1768..1802
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2436 AA;  280392 MW;  E6459FC03AEF796B CRC64;
     MSTTSASGKK KGPRLDEIKE KRERVLQRFN KFKDGSQDLK KKLEDARDFQ RFKRNVSELE
     EWIDEQMKIA NDESYKDPVN IQIKVKRHED FQGVIAKQKD VLDELVKEGS DMIDNEHLFF
     EQIQELLKQL LNHWEELDDK LSSKGAKLRE TQKLSAFTRE VDELLAWIAE KEAVASSDDY
     GRDLEHAEFL FKKFEEVQIE VKTGELRVEH VKEVAQPLID EDHPGKETVT ERIETVIVAW
     EKLLITIQIR HDKLLASVEK NRYKNAVEDA KQWIDERLAS VKDDDDPSNE ENAAAIKRKH
     DRIGNEVAAI EEKVNQLQAQ ANELCDKFPD DEDEIRAGSD SLDEKWNSLK DEVNMKRLKL
     NSGLNWLSLQ SRCKDYEMWA NTKKSDLAED ITKENISADV LEAQHEELKH EIRARNENLD
     ELLEECDQLL VSDHQSSDSI KNKMDLLKNL REELLEDWEE RNGVIEIMAS YQEYVRGVNQ
     VDSWMDKREP LLATDMPIES LDSAQALIKK HENFETTFTT QQEKAKTLYE SADKLVDENH
     YATEDIVNRK NKLEKHIQDT VLKAERRRHF LDDAHQYYNF VNVAEETIQW INEQITTVSD
     DSYKDLSNMQ GKLRKHQAFE AEVSANRTRI DNVNNSGKAL IEAEHPKTDK IEDKLDEING
     LWDKLVRLSS DKGSKLRDAH RELLFNREVD DMERWIAEVE LQLYSEDIGR DLVSVQNLIK
     KHTLLEADIA AHTEALKAIT EQADAFISEE HFHADSIKDK QQQVALRFSG LEDPVSERKA
     KLNDSLLLFQ FLRDVEDEET WIREKEAIAS SGSHGRDLLT VQSLIKKHQA MQTEIDNHET
     KIDAVCADGQ KLIDDEHYAT NDINDGINKL KDAWNLLKDK CIGRKSELDD SLRTHQYFAD
     SSEAEQWIKD KDQLTSSTDY GKDEDSAQSL LRKHDAVLSE IEAYGETIDN LRTASSKCKD
     IKPSASEVPP GTEMKALEDF DPDSSHELSL QKDDVVSVVH AANPKWWKVV KDDKVGFVPA
     SILMQVSDNS SETPLSPVSS LSPTVRPRSV SRLSVSRMSM MGPVELENVA SRQQALDDRY
     NALLKKARER RQKLVDSYKR HGLSREMSEL ETWIEEKKAA NTSAELGNDL DHVEALKQKF
     DDFLKDLEAN ETRVNEVNEV SQKLQNEGHS DAEAIRQQTL NLLENWDNLK KLTEKRRADL
     SGSHDIHKFF RDADETTSYI SEKVAVMSSD EVGRDLASVQ ALMRKHDGIE RDIAVLEDKI
     QGLDVEATKL AEIHPDSAER ICAKQSEIAE AWDNLVKQAA SRKAKLTDSQ DYQQFLNDHR
     DISSWINGMN SLVSSNELAH DVPGAETLLE VHLEHRTEID SRDESLQNLK NFGQSLIDKE
     HYASEDISEK LSSIQVDMQQ LENNWEFRKV RLDQCLGLQM FHRDAQQAES WMSVKENFFS
     TYDIAAQEDT TGSKKRENLD KAFALQEEKI NALRDMSDLL TEEGHYDAES IASKRDEILD
     RWNKLKDMLE SHRSKLGQTK TLNQFNLDAD EMEGWLNDKL KSLQDDSYQD PAFVQSKLQK
     QQALEAEVAA NEDRIKAVID MGNDLMANDA CSGNEEDVKK RIKDLEDQLL KLKEQMSEKN
     TRLKEASVLL QFTNTVKDLD FWFVQIEVLL TGEDYGKDLV TVSNILKKHQ VLLADVEVHA
     ERVEDLKKQG QDLIAGDHYG KDTIAEQIKD VADKFNKVKG LCAVRHDKLQ KSYILFQFYR
     DIEDEETWIS EKKLLMGSED YGKDLTSVQN LRKNHQRFQT ELSGHDNRIK NIQETADKLL
     NDESYPQADI KNRSESVSNL WMELKDAVAR RTEKLEQSYG YQQFMFDVEE EESWINEKFA
     MVNSDDYGDS LATVQNLLKK HEAFETDLEI RRDRVEKTVR DGEKLVNDGH YQSDNISARC
     QSLDSKLHVL INVAVTRKAG LRESHNFLQF KWKADVVESW IDDKENQIKS GDYGKDLSSV
     QALITKLDTF DSGLAAFEQE GIANLTSLKD DLIDSKHAKS DDIHARHKKV ADRWENLKNL
     SDDRRGRLLQ SQDKFKELED LFLTFAKKAS AFNSWYENAE EDLTDPVRCN SVEEIQALRG
     KHAQFKDSLA TEKNNLQQLR DLTKKIETYT RSSNPYTWFT MDAIEDSWKN IQSIVAERDG
     DLAKEEERQL QNDKLRQEFA KYANSFHTWL RETRANMVEG SGSLEDQLEN TKKISAEVTR
     RKTDLKKIED LGARLEEALI LDNKYTEHTT VGLAQQWDQL DQLGMRMQHN LEQQIEARNS
     SGVSEEQLNE FSTTFRHFDK DRSGKLDHAE FKSCLRSLGY DLPVVEEGEK DPEFEAILAS
     VDPNGDGFVT LEEYMAFMIS RETENVASKK DVEDAFKALT ADGDKPYIIG SELYQSLTKD
     QADYLVNNMP PYRNAHGDIV PDAFDYKAFT NMLFVS
//
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