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Protein

Hemocytin

Gene
N/A
Organism
Bombyx mori (Silk moth)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Adhesive protein and relates to hemostasis or encapsulation of foreign substances for self-defense.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Hemocytin
Alternative name(s):
Humoral lectin
OrganismiBombyx mori (Silk moth)
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
Proteomesi
  • UP000005204 Componenti: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000021445? – 3133Hemocytin
Signal peptidei1 – ?Sequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi? ↔ 3075By similarity
Glycosylationi151N-linked (GlcNAc...)Sequence analysis1
Glycosylationi237N-linked (GlcNAc...)Sequence analysis1
Glycosylationi564N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi940 ↔ 1095By similarity
Disulfide bondi1116 ↔ 1254By similarity
Glycosylationi1170N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1387N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1622N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1727N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1847N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1975N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1985N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2093N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2113N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2276N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2451N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2647N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2654N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2663N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2794N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2810N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2865N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2929N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2964N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2971 ↔ 3040By similarity
Disulfide bondi2991 ↔ 3054By similarity
Disulfide bondi3004 ↔ 3070By similarity
Disulfide bondi3020 ↔ 3072By similarity
Glycosylationi3028N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

May be converted into the 260 kDa mature hemocytin by proteolysis.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP98092.

Expressioni

Developmental stagei

Expressed in hemocytes during larval-pupal metamorphosis.

Inductioni

Hemagglutination activity is increased by bacterial or viral infection and inhibited by D-mannose, N-acetyl-D-galactosamine and D-maltose.

Structurei

3D structure databases

ProteinModelPortaliP98092.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 96TIL 1Add BLAST57
Domaini153 – 209TIL 2Add BLAST57
Domaini248 – 455VWFD 1PROSITE-ProRule annotationAdd BLAST208
Domaini509 – 576TIL 3Add BLAST68
Domaini770 – 837TIL 4Add BLAST68
Domaini940 – 1095F5/8 type C 1PROSITE-ProRule annotationAdd BLAST156
Domaini1116 – 1254F5/8 type C 2PROSITE-ProRule annotationAdd BLAST139
Domaini1619 – 1824VWFD 2PROSITE-ProRule annotationAdd BLAST206
Domaini1890 – 1948TIL 5Add BLAST59
Domaini1953 – 2179VWFD 3PROSITE-ProRule annotationAdd BLAST227
Domaini2229 – 2285TIL 6Add BLAST57
Domaini2553 – 2622VWFC 1Add BLAST70
Domaini2842 – 2907VWFC 2Add BLAST66
Domaini2971 – 3076CTCKPROSITE-ProRule annotationAdd BLAST106

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi895 – 914Poly-ThrAdd BLAST20
Compositional biasi1267 – 1270Poly-Glu4
Compositional biasi1425 – 1428Poly-Thr4
Compositional biasi1447 – 1450Poly-Thr4
Compositional biasi1474 – 1479Poly-Ser6
Compositional biasi2148 – 2153Poly-Pro6
Compositional biasi2156 – 2159Poly-Pro4
Compositional biasi2341 – 2344Poly-Pro4

Sequence similaritiesi

Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
Contains 2 VWFC domains.Curated
Contains 3 VWFD domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR7U. Eukaryota.
ENOG410YF4H. LUCA.
KOiK03900.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
InterProiIPR006207. Cys_knot_C.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR012111. Hml.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
[Graphical view]
PfamiPF08742. C8. 3 hits.
PF00754. F5_F8_type_C. 2 hits.
PF01826. TIL. 6 hits.
PF00094. VWD. 3 hits.
[Graphical view]
PIRSFiPIRSF036569. Hml. 1 hit.
SMARTiSM00832. C8. 3 hits.
SM00041. CT. 1 hit.
SM00231. FA58C. 2 hits.
SM00214. VWC. 5 hits.
SM00215. VWC_out. 1 hit.
SM00216. VWD. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF57567. SSF57567. 4 hits.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS51233. VWFD. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGGRDPVPV PVLGDYAMVC AKNGIILQWR YNVKECELSC TGGQQYTVCA
60 70 80 90 100
DSCLRKCSDT ALAASGQCKP VCVEGCACSP SQLLDDNGVC VPVAKCPCIH
110 120 130 140 150
KGLQFNAGYK EIRPGRRERE LCTCVGARWD CKPATPEEIQ NYPPAEDLRS
160 170 180 190 200
NSTAQNMEFT TCETSEPLTC KNMHLPPSTQ TAECRPGCQC KKGQVLDTAS
210 220 230 240 250
KRCVPATQCP CHHAGRSYPD GHLMQEECNK CECKNGNWSC TQRKCAGVCG
260 270 280 290 300
AWGDSHVNTF DGTQYDFEGV CTYLLAKGAM DGTDGFDVEI QNVPCGTTGA
310 320 330 340 350
TCSKSVTLKV GGAGNEEIVS LTKNAPIPDI SKLKRIKMRK AGAYVFLDVP
360 370 380 390 400
SLGMSLQWDR GLRVYVKIDT MWQGRVKGLC GNYNGDMRDD FQTPSGGGMS
410 420 430 440 450
ESSALIFADS WKLKPTCPKP QPVIDHCKQR PERKEWAQSV CGALKRYPFS
460 470 480 490 500
LCAGEVGAGA YVARCERDAC DAGADCECAC AALAAYAHAC AHRGVTFNWR
510 520 530 540 550
TNDLCPMQCD EVCSNYDSCV SACPVETCDN ILYYAETTAR CEQDTCVEGC
560 570 580 590 600
KPKKSCPEGS VYKNDSTTEC VPRAKCKPVC MTLDGGREVL EGEIIEEDAC
610 620 630 640 650
HTCRCSKKHK VCTGQPCSTE APRIQATSSS AEPATERPHE PLKCVTGWTP
660 670 680 690 700
WINRGPAEIG PDGQSVESEP LPKPNELQIG KPMCKPEMMK KIECRTVNDH
710 720 730 740 750
KTPKETGLNV ECSLENGLVC EEPEKTCPDF EIKVYCECEE PQDTSPPVTV
760 770 780 790 800
TSEASSEPVS TTLATTTSRC PPGEVYQACA YKCDRLCDHF KKTLIAKGRC
810 820 830 840 850
ISEMCVDGCV DESVASNGCE GSSRWRDERT CVPVKDCTCY NDGQIVKPGG
860 870 880 890 900
VTESGCIKCQ CLDNSLYCDS KDCVSLNIPH QGSTHLPYIV RPVSTTITST
910 920 930 940 950
TTTTTTSTTT TTTTPEPTET TTETTVPLII KSTVSPPPEC SPDNYIDLVM
960 970 980 990 1000
GDEPLPDTAF SASSEFSEIF APHNARLNRG PTNSGAGSWN PKVNNDKQYI
1010 1020 1030 1040 1050
QVELPRREPI YGVVLQGSPI FDQYVTSYEI MYGDDGNTFS TVDGPDGKPK
1060 1070 1080 1090 1100
IFRGPIDNTH PVKQMISPPI EAKVVRIRPL TWHDEISLRL EIIGCAEPLT
1110 1120 1130 1140 1150
TETSEPSPTS ESPLQCTEPL GLIGELPLEN IQVSSNSEEK DYLSINGNRG
1160 1170 1180 1190 1200
WKPLYNTPGW VMFDFTGPRN ITGILTKGGN DGWVTSYKVL YTSDFETFNP
1210 1220 1230 1240 1250
VIDKDGKEKI FPANFDGIVS VTNEFHPPIR ARYLKVLPQK WNKNIELRIE
1260 1270 1280 1290 1300
PIGCFEPYPE ILRSLPEEEE GREEPQVVRK EYGMSQEREM PNCHICPGVE
1310 1320 1330 1340 1350
AKECTCSYPE YFDGENCVPR AECPCVESFM TYPVGSTFRG ANCDECVCKL
1360 1370 1380 1390 1400
GGTTECKPFK ECQCDDESLV PKLSPTTCDC TCEPCTNGTK ICKTSKLCLA
1410 1420 1430 1440 1450
LESWCDGVQD CPDDERDCTT STARTTTTEP TVVTTVAPTQ AATAPPTTTT
1460 1470 1480 1490 1500
PKPVVECPKV ECPPGYIISY TTGSSSSYSR AFSSDLPPPR PRYSYQRYYR
1510 1520 1530 1540 1550
GRSTGGYSGY AKTGYSKGGF SKGGFSKGGY GYPSIPRSNQ AFTLDKPALT
1560 1570 1580 1590 1600
NKQPTSKEEC AQFKCISKLP AFKPGVVPPP VACSVVTCPA GYTLKLDKVP
1610 1620 1630 1640 1650
TGYNKCPQYE CVPPLERPVF CNMTGRTFNT FDGMEYKYDV CFHMLARDNK
1660 1670 1680 1690 1700
FDAWLIIVRK NCRLDGCTNE LIVMQDDQLI QVKPNMMVTY NNYEYTIEQT
1710 1720 1730 1740 1750
KKICFQKNSF DVDRLGNGIS ITSRKYNFTV LFNKEGDVKI GVLKKHMGGV
1760 1770 1780 1790 1800
DGLCGAYDGS LANERRLPDG RVATSIDEFG RSWAKPGVPA DACAPRVASA
1810 1820 1830 1840 1850
HKQRRAWDLC NVIAEEPFSQ CGKVLNLDKW RHICLEKICE CTDLVVNGTK
1860 1870 1880 1890 1900
RTEEQCRCLV LQQMAAECLA ADAGVDLASW RLMMDCPADC PPPLVHYDCY
1910 1920 1930 1940 1950
RKRCEETCAP YPNAARACPA QEGQCSPGCY CPDGKLRKGD QCVLPADCLD
1960 1970 1980 1990 2000
CTCTGVGTPA KYTTFEGDDL PFLGNCTYLA SRDRNQTGEH KYQVYATNGP
2010 2020 2030 2040 2050
CDDNANIVCT KIVHLIYEKN VIHISKDPTT KKLRTVIGKT AVFKYPVKEN
2060 2070 2080 2090 2100
WGTISLLNGQ DVSVTLPDIH VELTVSQLNL EFAVRVPTFL YGNRTEGLCG
2110 2120 2130 2140 2150
VCAGYQDFLV TSNGTVTDDF DLYGKSWQAS PEKLTELEVP SDEQCDAPPP
2160 2170 2180 2190 2200
PAPCTPPPPD NNTCYHLYNA DRFGACHALV EPQPYVESCE ADECGGHGPC
2210 2220 2230 2240 2250
DALQRYAAAC AELGLCLPDW RRELCPYPCE EPFVYRACVD CERTCDNYEQ
2260 2270 2280 2290 2300
LQTSPEKCTN KPVEGCFCPE GKVRVNNTCI EPGKCFPCGV DGHYAGDEWQ
2310 2320 2330 2340 2350
EDASTLCACA RSPHGTALVG CRATSCAPPV CAHGEDLRTA PPPPGQCCPE
2360 2370 2380 2390 2400
YDCVAKPEAQ CKETKKIVCD YGQVLKQKTN PSGCKEYFCE CKPSSECEVI
2410 2420 2430 2440 2450
PPESEVEIVE AGIHREIDNS GCCPRVSLVC RPETCPKPPH CPQFQTLASV
2460 2470 2480 2490 2500
NITGKCCPEY KCELPKDKCI VTLEWEAAAK GGEKPREKPQ TVLKDLEAVW
2510 2520 2530 2540 2550
LDGPCRSCEC ALSGAGPAAT CAVSACPAVV SSELFVLEPR PVPFACCPEP
2560 2570 2580 2590 2600
VQVACRHQDN VYKVGEKWKS PTDVCETYEC AADGDGKLQR LAAVQRCDRH
2610 2620 2630 2640 2650
CQPGWKYVPA EADSGQCCGK CEPVACVVDG EEKPIGEKWT SSDFCTNFTC
2660 2670 2680 2690 2700
VNLNGTLQVQ SSNETCPEIS DAERKQFVLK EQKVPGKCCP KIEREACTSG
2710 2720 2730 2740 2750
RSDIPGRREL DVDRELVREL PMRAGRGRRP ALRGLRAALR DRLPTRLEVL
2760 2770 2780 2790 2800
PAPAECCGRC KPSPASWKGG RGPSGRARER PVGESWTSAD FCTNYTCADL
2810 2820 2830 2840 2850
HGTLQVQSSN ETCPEVSEAV KKQFVLKEEK IPGKCCPKVE PVACRDGDKI
2860 2870 2880 2890 2900
YQEVQVWTTP DPCTNRTCRR EDGQLSVGRT VEHCERQCRR GWTYSPPAAD
2910 2920 2930 2940 2950
HCCGRCVQSA CLVDDQLKEP GSTWSSADNC TTFSCDRSGE EVFVTSATEH
2960 2970 2980 2990 3000
CPDVSACDPA DIVNTTCCQI CNEKPQALSK CVLRASELRH CRSDPHPMGA
3010 3020 3030 3040 3050
HGLCVNKFPI TGFTEVHGSC DSGTIYNNQT GTHESACECC QAAKYSGVSV
3060 3070 3080 3090 3100
RLTCEDGTVR PHRVATPARC HCAACGPGLT KHPKPGHASY TGTKNPVQPE
3110 3120 3130
RDREYVIPDI SSASGEARRN HDSNYITTLI ISF
Length:3,133
Mass (Da):343,355
Last modified:February 1, 1996 - v1
Checksum:iE5210D5D14A7B2B2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1288R → G.1
Natural varianti1305T → S.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29738 mRNA. Translation: BAA06160.1.
D14035 mRNA. Translation: BAA03124.1.
PIRiS52093.
RefSeqiNP_001104817.1. NM_001111347.1.
UniGeneiBmo.1330.

Genome annotation databases

GeneIDi692743.
KEGGibmor:692743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29738 mRNA. Translation: BAA06160.1.
D14035 mRNA. Translation: BAA03124.1.
PIRiS52093.
RefSeqiNP_001104817.1. NM_001111347.1.
UniGeneiBmo.1330.

3D structure databases

ProteinModelPortaliP98092.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP98092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi692743.
KEGGibmor:692743.

Phylogenomic databases

eggNOGiENOG410IR7U. Eukaryota.
ENOG410YF4H. LUCA.
KOiK03900.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
InterProiIPR006207. Cys_knot_C.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR012111. Hml.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
[Graphical view]
PfamiPF08742. C8. 3 hits.
PF00754. F5_F8_type_C. 2 hits.
PF01826. TIL. 6 hits.
PF00094. VWD. 3 hits.
[Graphical view]
PIRSFiPIRSF036569. Hml. 1 hit.
SMARTiSM00832. C8. 3 hits.
SM00041. CT. 1 hit.
SM00231. FA58C. 2 hits.
SM00214. VWC. 5 hits.
SM00215. VWC_out. 1 hit.
SM00216. VWD. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF57567. SSF57567. 4 hits.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS51233. VWFD. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHMCT_BOMMO
AccessioniPrimary (citable) accession number: P98092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 5, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.