SERI1_BOMMO
ID SERI1_BOMMO Reviewed; 1186 AA.
AC P07856; O96850; O96851; Q76B21; Q76B22; Q76B23;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Sericin 1;
DE AltName: Full=Silk gum protein;
DE Flags: Precursor;
GN Name=ser1;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1A' AND 1B).
RC STRAIN=Kinshu X Showa; TISSUE=Middle silk gland;
RX PubMed=14677702; DOI=10.1023/a:1026284620236;
RA Takahashi M., Tsujimoto K., Yamada H., Takagi H., Nakamori S.;
RT "The silk protein, sericin, protects against cell death caused by acute
RT serum deprivation in insect cell culture.";
RL Biotechnol. Lett. 25:1805-1809(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=15591204; DOI=10.1126/science.1102210;
RA Xia Q., Zhou Z., Lu C., Cheng D., Dai F., Li B., Zhao P., Zha X., Cheng T.,
RA Chai C., Pan G., Xu J., Liu C., Lin Y., Qian J., Hou Y., Wu Z., Li G.,
RA Pan M., Li C., Shen Y., Lan X., Yuan L., Li T., Xu H., Yang G., Wan Y.,
RA Zhu Y., Yu M., Shen W., Wu D., Xiang Z., Yu J., Wang J., Li R., Shi J.,
RA Li H., Li G., Su J., Wang X., Li G., Zhang Z., Wu Q., Li J., Zhang Q.,
RA Wei N., Xu J., Sun H., Dong L., Liu D., Zhao S., Zhao X., Meng Q., Lan F.,
RA Huang X., Li Y., Fang L., Li C., Li D., Sun Y., Zhang Z., Yang Z.,
RA Huang Y., Xi Y., Qi Q., He D., Huang H., Zhang X., Wang Z., Li W., Cao Y.,
RA Yu Y., Yu H., Li J., Ye J., Chen H., Zhou Y., Liu B., Wang J., Ye J.,
RA Ji H., Li S., Ni P., Zhang J., Zhang Y., Zheng H., Mao B., Wang W., Ye C.,
RA Li S., Wang J., Wong G.K.-S., Yang H.;
RT "A draft sequence for the genome of the domesticated silkworm (Bombyx
RT mori).";
RL Science 306:1937-1940(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5; 14-23 AND 25-95.
RC TISSUE=Middle silk gland;
RX PubMed=6294094; DOI=10.1016/s0021-9258(18)33412-4;
RA Okamoto H., Ishikawa E., Suzuki Y.;
RT "Structural analysis of sericin genes. Homologies with fibroin gene in the
RT 5' flanking nucleotide sequences.";
RL J. Biol. Chem. 257:15192-15199(1982).
RN [4]
RP PROTEIN SEQUENCE OF 37-49; 73-85; 122-139; 305-322; 427-444; 489-504;
RP 515-606; 612-889; 906-1006; 1049-1148 AND 1166-1186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (AUG-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE OF 647-683 AND 761-798.
RX PubMed=3024742; DOI=10.1016/s0300-9084(86)80060-8;
RA Michaille J.-J., Couble P., Prudhomme J.-C., Garel A.;
RT "A single gene produces multiple sericin messenger RNAs in the silk gland
RT of Bombyx mori.";
RL Biochimie 68:1165-1173(1986).
RN [6]
RP BIOTECHNOLOGICAL RELEVANCE.
RX PubMed=14538058; DOI=10.1016/s0734-9750(02)00003-4;
RA Zhang Y.Q.;
RT "Applications of natural silk protein sericin in biomaterials.";
RL Biotechnol. Adv. 20:91-100(2002).
CC -!- FUNCTION: Provides the silk fibroin thread with a sticky coating. Acts
CC as a cement by sticking silk threads together.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1B;
CC IsoId=P07856-1; Sequence=Displayed;
CC Name=1A;
CC IsoId=P07856-2; Sequence=VSP_012702;
CC Name=1A';
CC IsoId=P07856-3; Sequence=VSP_012703;
CC -!- TISSUE SPECIFICITY: Produced exclusively in the middle (MSG) section of
CC silk glands.
CC -!- BIOTECHNOLOGY: Sericin is useful because of its properties. The protein
CC resists oxidation, is antibacterial, UV resistant, and absorbs and
CC releases moisture easily. Sericin can be cross-linked, copolymerized,
CC and blended with other macromolecular materials, especially artificial
CC polymers, to produce materials with improved properties. The protein is
CC also used as an improving reagent or a coating material for natural and
CC artificial fibers, fabrics, and articles. The materials modified with
CC sericin and composites are useful as degradable biomaterials,
CC biomedical materials, polymers for forming articles, functional
CC membranes, fibers, and fabrics. {ECO:0000269|PubMed:14538058}.
CC -!- MISCELLANEOUS: The glue-like property of sericin is attributed to the
CC hydrogen bonding between serine residues of sericin with serine
CC residues in the fibroin structural components of silk fiber.
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DR EMBL; AB112019; BAD00698.1; -; mRNA.
DR EMBL; AB112020; BAD00699.1; -; mRNA.
DR EMBL; AB112021; BAD00700.1; -; mRNA.
DR EMBL; AADK01002558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M26101; AAA27843.1; -; mRNA.
DR EMBL; M26102; AAA27844.1; -; mRNA.
DR EMBL; M26103; AAA27845.1; -; mRNA.
DR EMBL; M26104; AAA27846.1; -; mRNA.
DR AlphaFoldDB; P07856; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Reference proteome;
KW Repeat; Secreted; Signal; Silk protein.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1186
FT /note="Sericin 1"
FT /id="PRO_0000022321"
FT REPEAT 593..630
FT /note="1"
FT REPEAT 631..668
FT /note="2"
FT REPEAT 669..706
FT /note="3"
FT REPEAT 707..744
FT /note="4"
FT REPEAT 745..782
FT /note="5"
FT REPEAT 783..820
FT /note="6"
FT REPEAT 821..858
FT /note="7"
FT REPEAT 859..896
FT /note="8"
FT REPEAT 897..934
FT /note="9"
FT REPEAT 935..972
FT /note="10"
FT REPEAT 973..1010
FT /note="11"
FT REGION 39..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 24..461
FT /note="PGNRDTVEVKNRKYNAASSESSYLNKDNDSISAGAHRAKSVEQSQDKSKYTS
FT GPEGVSYSGRSQNYKDSKQAYADYHSDPNGGSASAGQSRDSSLRERNVHYVSDGEAVAA
FT SSDARDENRSAQQNAQANWNADGSYGVSADRSGSASSRRRQANYYSDKDITAASKDDSR
FT ADSSRRSNAYYNRDSDGSESAGLSDRSASSSKNDNVFVYRTKDSIGGQAKSSRSSHSQE
FT SDAYYNSSPDGSYNAGTRDSSISNKKKASSTIYADKDQIRAANDRSSSKQLKQSSAQIS
FT SGPEGTSVSSKDRQYSNDKRSKSDAYVGRDGTVAYSNKDSEKTSRQSNTNYADQNSVRS
FT DSAASDQTSKSYDRGYSDKNIVAHSSGSRGSQNQKSSSYRADKDGFSSSTNTEKSKFSS
FT SNSVVETSDGASASRESSAEDTKSSNSNVQSD -> QTGEEEELFDVVSYQKIEDGKPV
FT IIMKVIPV (in isoform 1A)"
FT /evidence="ECO:0000303|PubMed:14677702"
FT /id="VSP_012702"
FT VAR_SEQ 25..488
FT /note="Missing (in isoform 1A')"
FT /evidence="ECO:0000303|PubMed:14677702"
FT /id="VSP_012703"
FT CONFLICT 50
FT /note="D -> A (in Ref. 1; BAD00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="H -> R (in Ref. 1; BAD00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="V -> A (in Ref. 1; BAD00699)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="G -> E (in Ref. 1; BAD00699)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="L -> S (in Ref. 1; BAD00699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1186 AA; 119486 MW; F6399DD3AE938D2E CRC64;
MRFVLCCTLI ALAALSVKAF GHHPGNRDTV EVKNRKYNAA SSESSYLNKD NDSISAGAHR
AKSVEQSQDK SKYTSGPEGV SYSGRSQNYK DSKQAYADYH SDPNGGSASA GQSRDSSLRE
RNVHYVSDGE AVAASSDARD ENRSAQQNAQ ANWNADGSYG VSADRSGSAS SRRRQANYYS
DKDITAASKD DSRADSSRRS NAYYNRDSDG SESAGLSDRS ASSSKNDNVF VYRTKDSIGG
QAKSSRSSHS QESDAYYNSS PDGSYNAGTR DSSISNKKKA SSTIYADKDQ IRAANDRSSS
KQLKQSSAQI SSGPEGTSVS SKDRQYSNDK RSKSDAYVGR DGTVAYSNKD SEKTSRQSNT
NYADQNSVRS DSAASDQTSK SYDRGYSDKN IVAHSSGSRG SQNQKSSSYR ADKDGFSSST
NTEKSKFSSS NSVVETSDGA SASRESSAED TKSSNSNVQS DEKSASQSSS SRSSQESASY
SSSSSSSTLS EDSSEVDIDL GNLGWWWNSD NKVQRAAGGA TKSGASSSTQ ATTVSGADDS
ADSYTWWWNP RRSSSSSSSA SSSSSGSNVG GSSQSSGSST SGSNARGHLG TVSSTGSTSN
TDSSSKSAGS RTSGGSSTYG YSSSHRGGSV SSTGSSSNTD SSTKNAGSST SGGSSTYGYS
SSHRGGSVSS TGSSSNTDSS TKSAGSSTSG GSSTYGYSSR HRGGRVSSTG SSSTTDASSN
SVGSSTSGGS STYGYSSNSR DGSVSSTGSS SNTDSNSNSA GSSTSGGSST YGYSSNSRDG
SVSSTGSSSN TDSNSNSAGS STSGGSSTYG YSSNSRDGSV SSTGSSSNTD ASTDLTGSST
SGGSSTYGYS SDSRDGSVSS TGSSSNTDAS TDLAGSSTSG GSSTYGYSSD CGDGSVSSTG
SSSNTDASTD LAGSSTSGGS STYGYSSDSR DGSVSSTGSS SNTDASTDLA GSSTSGGSST
YGYSSNSRDG SVSSTGSSSN TDASTDLTGS STSGGSSTYG YSSSNRDGSV LATGSSSNTD
ASTTEESTTS AGSSTEGYSS SSHDGSVTST DGSSTSGGAS SSSASTAKSD AASSEDGFWW
WNRRKSGSGH KSATVQSSTT DKTSTDSASS TDSTSSTSGA STTTSGSSST SGGSSTSDAS
STSSSVSRSH HSGVNRLLHK PGQGKICLCF ENIFDIPYHL RKNIGV
