ID C3ZT72_BRAFL Unreviewed; 963 AA.
AC C3ZT72;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Sushi domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_86715 {ECO:0000313|EMBL:EEN44278.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN44278.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN44278.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN44278.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; GG666676; EEN44278.1; -; Genomic_DNA.
DR RefSeq; XP_002588267.1; XM_002588221.1.
DR AlphaFoldDB; C3ZT72; -.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; C3ZT72; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd18989; LGIC_ECD_cation; 1.
DR CDD; cd19051; LGIC_TM_cation; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR46335; CUBILIN; 1.
DR PANTHER; PTHR46335:SF3; CUBILIN HOMOLOG; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR Pfam; PF00084; Sushi; 1.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 729..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 942..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 405..478
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 471..543
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 252..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 963 AA; 105013 MW; CE547FF4DDCCB79D CRC64;
MQLMPTPTLA STVQASVTNV QPSTATLHPR TVTVQPGTTT MQSSTAAQHQ RLCRQAPRLC
SPVPRLCRQA PRLCSPAPHA QLCSPAPRLC TLAPRLCSPA HDFAARHRRT TLQPSTATVQ
ASTATVQPST ARTALPPSTA TVHSSTTTVQ PSTTTVPPGT ARTTLPPSTA TVQASTTTVQ
PSTARTTLPP CSTTVQPSTM TVQPRTATLQ PSTTTLQPST ARTTLQGINA ELPSGYHQCA
HGNACILAWK RCDGLTDCTD GSDEGSCVCL STPEDLNLGG RLAMLPNQLG QTTFKEILNS
SAVDFLSSSS SNTENRHPGF REFASAVIFP RCLLYEDNNT FCSSSLHGDN KTSCITQLVP
CRSWCEEVLH MADDRLKNRF PTCDLFPSPP HACWNPEPET KNNEVCYHGS GINYRGAWSK
TASGVECVEW STAQAGFYKT EYPWANLENN YCRNPTGHER PFCLVEDGSQ EECDVIPCNV
VGCWDLGPPN YGKRIPVKRF YNVGEKVAYT CDVGYSLENG SYSDMRCTEG GIWEPDDKPS
CSVDIRGKLE EDLFVVYSPN QAPKTENRSL SVISFKGSVE QIVDLTWQDS RLKWEPEYYR
NIETISVPGS SIWIPTLTLK RNADPSYPGL PKDVPLLITI DGTVTWRVET LTSTICDADP
FLFPADTMEC HICFSVSSAI RHTIECGGES TCDVWSPTQQ EGEWKRKDKI FTEGNKTACF
AVHLKRIPLF HIATTVAPCV ILAVLMTITF VMPIDKGDRI SFGVTILLSM VVSLVFVTDV
LPVKGALPFF ASLIVVYMAM MGLFLFFTIY IITLHDKEGG LSPMAKTFFL RYMAGFLLLG
DLTEKEAASD DGETGHTGGK LAWPKRTNRV APADGVAEAN VETPADVSGT PCQPSGPPSR
LEAAMTSGFS NLIHSVEELT KAVKNEPEVS DYTLLTKVLD RLCLVLYVIS VAVAVPMTMY
LTK
//
