ID C3ZER7_BRAFL Unreviewed; 1601 AA.
AC C3ZER7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Deleted in malignant brain tumors 1 protein {ECO:0000256|ARBA:ARBA00014650};
DE AltName: Full=Hensin {ECO:0000256|ARBA:ARBA00030560};
GN ORFNames=BRAFLDRAFT_120140 {ECO:0000313|EMBL:EEN49223.1};
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:EEN49223.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49223.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN49223.1};
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 -!- SIMILARITY: Belongs to the DMBT1 family.
CC {ECO:0000256|ARBA:ARBA00009931}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; GG666612; EEN49223.1; -; Genomic_DNA.
DR RefSeq; XP_002593212.1; XM_002593166.1.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR InParanoid; C3ZER7; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd06263; MAM; 3.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 7.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR048290; ZP_chr.
DR InterPro; IPR001507; ZP_dom.
DR PANTHER; PTHR48071:SF18; LCCL_LECTIN ADHESIVE-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00629; MAM; 3.
DR Pfam; PF00530; SRCR; 7.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00137; MAM; 3.
DR SMART; SM00202; SR; 6.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF56487; SRCR-like; 7.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00740; MAM_1; 2.
DR PROSITE; PS50060; MAM_2; 3.
DR PROSITE; PS00420; SRCR_1; 3.
DR PROSITE; PS50287; SRCR_2; 7.
DR PROSITE; PS51034; ZP_2; 1.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..37
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 69..168
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 175..327
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 332..431
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 436..537
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 480..658
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 654..817
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 861..961
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1005..1113
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1115..1215
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1236..1335
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1361..1601
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT DISULFID 6..16
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 93..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 106..167
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 137..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 356..420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 369..430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 400..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 504..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 886..950
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 899..960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 930..940
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1140..1204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1153..1214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1184..1194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1305..1315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1601 AA; 178974 MW; 5D1BA64994585AE4 CRC64;
MDDVKCSGTE PSLEYCDQRG WGSHNCDHSE DVGLICDAPV TTTEMQPTTI PQTTLYPDNG
IITFSGFSVR LSSGGPNYGR VEVLVNGTWG TVCDDRFGAD EARVVCQELG FRDYISFDGG
AHYGLGTGPI WMDDVQCTGY EPSIQFCQHR GWGVENCGHH EDVGVECQGP DRTLIDCDFD
TNRCNFTGDA TADFEWRRRA GRTPSASTGP SFDHTTGSGY YMYIEASSPR QPGDTARLVS
PVLNAYGTHC LQFAYHLYGD SIGELKVLVG SEVVFFRNAS DGDFWQEAKM DVSLNNNQIT
FEGVVGIGWR GDVAIDDVLL YSGSCQSNDY DIRLEDGGYS YGRVEVRVNG EWGTICDDGF
GEPEAAVICR ELGFAGVEAF YPGAYYGEGT GKIWLSDVKC SGDESAIRQC GHADWGVNSC
LHAQDISVDC KQEIEVRLAD GDTNYGRVEV KYDGQWGTIC DDDFGESEAR VICRQLGFPD
FETFHYGAYY GPGTGPVWLS NLQCNGFETN VEDCSHSGWG MNPPTCTHPH DVSVVCQGSG
YYVYTESAEL APGDASFLLS PVASLNVPSQ SCLRFSYHMY GTDIGELKLY VQNGSGNWYQ
PFDRSGDQGD AWITENIDLN APVGQVMFIG IRKSIVGAGL AGDIGVDDIR HYWGPCNLEL
GQSGGNKMAV LWVILHLILV LSDGIASGEE ANDDGDNRES RWYTDYTTWG YYMYIEASSG
SPGNIARLVS PTIFDNGWYC LQFAYHMYGT DINQLRVLVG SSVVWSLSNN RGTSWHLASR
EVYIRNTQIV FEGVRGSSYQ GDIAIDDVTL YPGYCPWTDN PGTYAYYTEE TTAAPSTWWW
TTAWNNWWTT ANTDYYYNFQ VRLRGGDYYS YGRVEVYYNG QWGTVCDDGF GWNEANVVCH
ELGFDQVDTY YHNAHYGSGS GPIWLDDLNC YGSESSLQYC PHRGWGSHNC GHGNDVSVSC
VEPSRTDMET STISIPQTPG WWELTTNYWD WWRTTSYNRP PHVPCGGHIT QSSGVIQSPH
YPNNYFNRAD CQWTIIRSPG STVQVVVERY DMESCCDHLD IYDGRYNSSR RLARLNGSGS
WRYYYSSSNE VLIHFTSDYS VVDNGFRIRF QDFQIRLRGG DNYSYGRVEV YYSGYWGTVC
DDNFGWQDAR VVCRELGFPD YYSYQQNAYY GQGSGPIWMD DLGCSGSENS LQYCPHLGWG
SHNCGHSEDI GVRCSCRLQF CTAFVIIGTR NGHFQVRLRG GNSYSYGRVE VYYNGQWGTV
CDHEFGWEEA RVVCRELGFS DYINYYHNAY YGQGSGPIWM DHLRCSGYES SLQYCPHDGW
GTHCGHSDDI SVLCGNANVT DVSTVIPPWH TSQPDLGMTG SCDSDMMTVT FDLWVAPWLD
GNLMHFADPT CKAINNGSHL ILATKLSDCG TTRNETDDYV IYSNKVLMYS SNHSVIIRDL
QLEVPVTCKL PRKSVVSAQF TADSNAIKYS LEREGNFDIE LQFYDSLSFY YAYTGPVGLQ
LNELAYAQVR LSSDDNLRIM VDSCVATPSR NPADTVIYSV IENNCPKDPT VMTYYTSSPK
VERFGFRAFQ FATGQNQVFL HCLVQVCDGV RPQLAVHPGD A
//
