SALM_DROVI
ID SALM_DROVI Reviewed; 1402 AA.
AC P39806;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Homeotic protein spalt-major;
GN Name=salm;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7905822; DOI=10.1002/j.1460-2075.1994.tb06246.x;
RA Kuehnlein R.P., Frommer G., Friedrich M., Gonzalez-Gaitan M., Weber A.,
RA Wagner-Bernholz J.F., Gehring W.J., Jaeckle H., Schuh R.;
RT "Spalt encodes an evolutionarily conserved zinc finger protein of novel
RT structure which provides homeotic gene function in the head and tail region
RT of the Drosophila embryo.";
RL EMBO J. 13:168-179(1994).
CC -!- FUNCTION: Required for the establishment of the posterior-most head and
CC the anterior-most tail segments of the embryo. Probably function as a
CC transcriptional regulator. Could repress the transcription of the tsh
CC gene.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: First expressed at blastoderm stage and later in
CC restricted aeras of the embryonic nervous system as well as in the
CC developing trachea.
CC -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; Z27444; CAA81800.1; -; mRNA.
DR PIR; S42748; S42748.
DR PRIDE; P39806; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1402
FT /note="Homeotic protein spalt-major"
FT /id="PRO_0000047019"
FT ZN_FING 432..454
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 845..867
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 873..895
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 905..927
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1336..1358
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1364..1386
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 24..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..268
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 153746 MW; 4CDB2EE384F70AE5 CRC64;
MRSDFKDNHQ ETINKMIQFG TVKYGIVKQL KDPARSAEKD IASDQEDNGA CSPLTTANAS
ASAGNSPCPS RSPQQHSEDE REPEQVSEQE LVPEVSAQSE SEIGEEIENN ADETNADHNH
NNNNNNKLVM TKPPVEHEVE QNANLNASMP NSTTPPATNA VIAGARAQQF GATPVTLEAI
QNMQMAIAQF AAKTIANGAS GTDNEAAMKQ LAFLQQTLFN LQQQQLFQLQ LIQQLQSQLA
LNQVKQNDDE ADEELEPEER EDGETDTYEE EERIADMELR QKAEARMAES KARQHLINAG
VPYANAPDPS HQPPHRCRLR RLKRKREEDA SAKSSGASAK IFGEQESSQD ALNKLKEMEN
MPLPFGADLS SSIITNHDDL PEPNSLDLLQ KRTQEVLDSA SQGILANNMA DDFAFGDKSS
DGKGRNEPFF KHRCRYCGKV FGSDSALQIH IRSHTGERPF KCNVCGSRFT TKGNLKVHFQ
RHAQKFPHVP MNATPIPEHM DKFHPPLLDQ MSPDSSPTQS PAPATGLPPP STSTLTQMQP
SMSFASSPAF PGLPGIYRPP MELLKSLGAT AGSTAGLPHP FFPQMPGLGA ALKHTHDQSQ
DMPTDLRKSS GPSSPHEEED NIAARLPVKS ELMEEEKTEH TMEAATRESA EMEPLPLEVR
IKEERIDEDQ MHLQEGMQKP EPLTAYATPH PQQCLIPTTH AAAKSPRSLP LQCHARLSLW
CSHPTTSNHA CAVLTGSQTH LDQLPTPDNV PPTMPQREDF FAERFPLNFT SKTDDHSPIR
SPAGHAHAHI PRSPFFNPIK HEMAAFVPRP HSNDNSWENF IEVSNTSETM KLKELMKNKK
ISDPNQCVVC DRVLSCKSAL QMHYRTHTGE RPFKCRICGR AFTTKGNLKT HMAVHKIRPP
MRNFHQCPVC HKKYSNALVL QQHIRLHTGE PTDLTPEQIQ AAEIRDPPPS MMPGHFMNPF
AAAAFHFGAM PGGGAGGPPG ATGMPGGPHN GTLGSESSQG DLDDNMDCGD GDDFDDISSE
HLSNSNDPAA TSDRRSSDDF KSLLFEQKLR IDPTGVVNIN SHQRPHSAAS NPNSIGSASA
SPSAPTSPSS QPKPSCSPVR SSCSPVRSVS ETSQGALDLT PRALPPPLAS SSSRSPYRQL
LSVRRRPLAR SVSSHRCVVP MVRALLSSQL PPSVGIDCLP PGLQHHLQQQ HQHLMQQQXA
VAAAAAAQHH HHQMQQHAAA LHQHQEHLRR EAQEVQQKAA QEVQQKAAAA AAAAAAAQRQ
ESPQPPPRSG ESSVGPPAQP NPLISARPPF GMFPNLPIFP PATTQNMCNA MNQIAQSVMP
AAPFNPLALS GVRGSTTCGI CYKTFPCHSA LEIHYRSHTK ERPFKCNICD RGFTTKGNLK
QHMLTHKIRD MEQETFRNRA VK
