We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - Q10583 (HCY1_MEGCR)
Protein
Hemocyanin 1
Gene
KLH1
Organism
Megathura crenulata (Giant keyhole limpet)
Status
Functioni
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 17 | Divalent metal cation; structural1 Publication | 1 | |
Metal bindingi | 58 | Copper 1; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 76 | Copper 1; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 85 | Copper 1; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 195 | Copper 2; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 199 | Copper 2; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 226 | Copper 2; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 478 | Copper 3; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 498 | Copper 3; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 507 | Copper 3; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 618 | Copper 4; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 622 | Copper 4; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 649 | Copper 4; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 737 | Divalent metal cation; structural1 Publication | 1 | |
Metal bindingi | 892 | Copper 5; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 912 | Copper 5; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 921 | Copper 5; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1031 | Copper 6; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1035 | Copper 6; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1062 | Copper 6; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1309 | Copper 7; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1327 | Copper 7; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1336 | Copper 7; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1440 | Copper 8; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1444 | Copper 8; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1471 | Copper 8; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1721 | Copper 9; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1741 | Copper 9; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1750 | Copper 9; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1863 | Copper 10; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1867 | Copper 10; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 1894 | Copper 10; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2138 | Copper 11; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2157 | Copper 11; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2166 | Copper 11; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2276 | Copper 12; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2280 | Copper 12; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2307 | Copper 12; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2424 | Divalent metal cation; structural1 Publication | 1 | |
Metal bindingi | 2558 | Copper 13; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2577 | Copper 13; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2586 | Copper 13; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2686 | Copper 14; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2690 | Copper 14; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2717 | Copper 14; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2962 | Copper 15; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2981 | Copper 15; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 2990 | Copper 15; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 3091 | Copper 16; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 3095 | Copper 16; via tele nitrogenCombined sources | 1 | |
Metal bindingi | 3122 | Copper 16; via tele nitrogenCombined sources | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- oxidoreductase activity Source: InterPro
- oxygen carrier activity Source: UniProtKB-KW
Keywordsi
Biological process | Oxygen transport, Transport |
Ligand | Copper, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Hemocyanin 1ImportedAlternative name(s): Keyhole limpet hemocyanin A1 Publication Short name: KLH-A1 Publication |
Gene namesi | Name:KLH11 Publication |
Organismi | Megathura crenulata (Giant keyhole limpet) |
Taxonomic identifieri | 55429 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Spiralia › Lophotrochozoa › Mollusca › Gastropoda › Vetigastropoda › Lepetellida › Fissurelloidea › Fissurellidae › Megathura |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPathology & Biotechi
Biotechnological usei
Potent immunogen used classically as a carrier protein for haptens and more recently in human vaccines and for immunotherapy of bladder cancer.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 16 | Sequence analysisAdd BLAST | 16 | |
ChainiPRO_0000204304 | 17 – 3414 | Hemocyanin 1Add BLAST | 3398 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 64 ↔ 73 | Combined sources | ||
Cross-linki | 74 ↔ 76 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Disulfide bondi | 185 ↔ 252 | Combined sources | ||
Cross-linki | 287 ↔ 290 | 2'-(S-cysteinyl)-histidine (Cys-His)1 Publication | ||
Disulfide bondi | 339 ↔ 351 | Combined sources | ||
Glycosylationi | 403 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 484 ↔ 495 | Combined sources | ||
Cross-linki | 496 ↔ 498 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Glycosylationi | 545 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 608 ↔ 674 | Combined sources | ||
Disulfide bondi | 898 ↔ 909 | Combined sources | ||
Cross-linki | 910 ↔ 912 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Disulfide bondi | 1021 ↔ 1088 | Combined sources | ||
Disulfide bondi | 1178 ↔ 1184 | Combined sources | ||
Disulfide bondi | 1315 ↔ 1324 | Combined sources | ||
Cross-linki | 1325 ↔ 1327 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Disulfide bondi | 1430 ↔ 1497 | Combined sources | ||
Disulfide bondi | 1585 ↔ 1595 | Combined sources | ||
Glycosylationi | 1648 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 1727 ↔ 1738 | Combined sources | ||
Cross-linki | 1739 ↔ 1741 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Disulfide bondi | 1853 ↔ 1920 | Combined sources | ||
Disulfide bondi | 2009 ↔ 2015 | Combined sources | ||
Disulfide bondi | 2144 ↔ 2154 | Combined sources | ||
Glycosylationi | 2145 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Cross-linki | 2155 ↔ 2157 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Disulfide bondi | 2266 ↔ 2333 | Combined sources | ||
Disulfide bondi | 2420 ↔ 2426 | Combined sources | ||
Disulfide bondi | 2564 ↔ 2574 | Combined sources | ||
Glycosylationi | 2571 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Cross-linki | 2575 ↔ 2577 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Disulfide bondi | 2676 ↔ 2743 | Combined sources | ||
Disulfide bondi | 2830 ↔ 2836 | Combined sources | ||
Disulfide bondi | 2968 ↔ 2978 | Combined sources | ||
Cross-linki | 2979 ↔ 2981 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity1 Publication | ||
Disulfide bondi | 3081 ↔ 3148 | Combined sources | ||
Glycosylationi | 3278 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 3367 ↔ 3400 | Combined sources |
Post-translational modificationi
Probably N-glycosylated (Probable). Asn-1280 and Asn-2484 are buried deeply in the protein which make them inaccessible for sugar attachment (Probable). Asn-3278 N-glycan is likely to represent a diantennate carbohydrate tree (Probable). The didecamer is almost evenly tagged by a total of 120 sugar trees (Probable).1 Publication
Keywords - PTMi
Disulfide bond, Glycoprotein, Thioether bondPTM databases
GlyConnecti | 211, 15 N-Linked glycans |
Expressioni
Tissue specificityi
Hemolymph.1 Publication
Interactioni
Subunit structurei
Homo-didecamer, with two decamers assembled face-to-face at their open ends. This didecamer form a stable 25 nM cylinder wall.
1 PublicationFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 628 – 669 | WD 1Sequence analysisAdd BLAST | 42 | |
Repeati | 1041 – 1082 | WD 2Sequence analysisAdd BLAST | 42 | |
Repeati | 1450 – 1491 | WD 3Sequence analysisAdd BLAST | 42 | |
Repeati | 1873 – 1914 | WD 4Sequence analysisAdd BLAST | 42 | |
Repeati | 2163 – 2199 | WD 5Sequence analysisAdd BLAST | 37 | |
Repeati | 2696 – 2737 | WD 6Sequence analysisAdd BLAST | 42 | |
Repeati | 3101 – 3142 | WD 7Sequence analysisAdd BLAST | 42 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 17 – 437 | Functional unit a (wall)1 PublicationAdd BLAST | 421 | |
Regioni | 438 – 851 | Functional unit b (wall)1 PublicationAdd BLAST | 414 | |
Regioni | 852 – 1271 | Functional unit c (wall)1 PublicationAdd BLAST | 420 | |
Regioni | 1272 – 1680 | Functional unit d (wall)1 PublicationAdd BLAST | 409 | |
Regioni | 1681 – 2097 | Functional unit e (wall)1 PublicationAdd BLAST | 417 | |
Regioni | 2098 – 2517 | Functional unit f (wall)1 PublicationAdd BLAST | 420 | |
Regioni | 2518 – 2921 | Functional unit g (internal arc)1 PublicationAdd BLAST | 404 | |
Regioni | 2922 – 3414 | Functional unit h (internal slab)1 PublicationAdd BLAST | 493 |
Domaini
The protein is composed of 8 globular functional units (a->h), forming a 'pearl chain'. Each unit is separated from the next by a linker. Since the lengths but not the exact positions are known, lengths are indicated here in free text. Linker lengths in amino acids are: 20 (a->b), 13 (b->c), 19 (c->d), 16 (d->e), 14 (e->f), 17 (f->g), and 17 (g->h).1 Publication
Sequence similaritiesi
Keywords - Domaini
Repeat, Signal, WD repeatFamily and domain databases
Gene3Di | 1.10.1280.10, 8 hits 2.60.310.10, 8 hits |
InterProi | View protein in InterPro IPR028999, Haemocyanin_beta-sandwich IPR036848, Haemocyanin_C_sf IPR002227, Tyrosinase_Cu-bd IPR008922, Unchr_di-copper_centre |
Pfami | View protein in Pfam PF14830, Haemocyan_bet_s, 8 hits PF00264, Tyrosinase, 9 hits |
PRINTSi | PR00092, TYROSINASE |
SUPFAMi | SSF48056, SSF48056, 8 hits SSF81277, SSF81277, 8 hits |
PROSITEi | View protein in PROSITE PS00497, TYROSINASE_1, 7 hits PS00498, TYROSINASE_2, 8 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q10583-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLSVRLLIVV LALANAENLV RKSVEHLTQE ETLDLQAALR ELQMDSSSIG
60 70 80 90 100
FQKIAAAHGA PASCVHKDTS IACCIHGMPT FPHWHRAYVV HMERALQTKR
110 120 130 140 150
RTSGLPYWDW TEPITQLPSL AADPVYIDSQ GGKAHTNYWY RGNIDFLDKK
160 170 180 190 200
TNRAVDDRLF EKVKPGQHTH LMESVLDALE QDEFCKFEIQ FELAHNAIHY
210 220 230 240 250
LVGGKHDYSM ANLEYTAYDP IFFLHHSNVD RIFAIWQRLQ ELRNKDPKAM
260 270 280 290 300
DCAQELLHQK MEPFSWEDND IPLTNEHSTP ADLFDYCELH YDYDTLNLNG
310 320 330 340 350
MTPEELKTYL DERSSRARAF ASFRLKGFGG SANVFVYVCI PDDNDRNDDH
360 370 380 390 400
CEKAGDFFVL GGPSEMKWQF YRPYLFDLSD TVHKMGMKLD GHYTVKAELF
410 420 430 440 450
SVNGTALPDD LLPHPVVVHH PEKGFTDPPV KHHQSANLLV RKNINDLTRE
460 470 480 490 500
EVLNLREAFH KFQEDRSVDG YQATAEYHGL PARCPRPDAK DRYACCVHGM
510 520 530 540 550
PIFPHWHRLF VTQVEDALVG RGATIGIPYW DWTEPMTHIP GLAGNKTYVD
560 570 580 590 600
SHGASHTNPF HSSVIAFEEN APHTKRQIDQ RLFKPATFGH HTDLFNQILY
610 620 630 640 650
AFEQEDYCDF EVQFEITHNT IHAWTGGSEH FSMSSLHYTA FDPLFYFHHS
660 670 680 690 700
NVDRLWAVWQ ALQMRRHKPY RAHCAISLEH MHLKPFAFSS PLNNNEKTHA
710 720 730 740 750
NAMPNKIYDY ENVLHYTYED LTFGGISLEN IEKMIHENQQ EDRIYAGFLL
760 770 780 790 800
AGIRTSANVD IFIKTTDSVQ HKAGTFAVLG GSKEMKWGFD RVFKFDITHV
810 820 830 840 850
LKDLDLTADG DFEVTVDITE VDGTKLASSL IPHASVIREH ARVKFDKVPR
860 870 880 890 900
SRLIRKNVDR LSPEEMNELR KALALLKEDK SAGGFQQLGA FHGEPKWCPS
910 920 930 940 950
PEASKKFACC VHGMSVFPHW HRLLTVQSEN ALRRHGYDGA LPYWDWTSPL
960 970 980 990 1000
NHLPELADHE KYVDPEDGVE KHNPWFDGHI DTVDKTTTRS VQNKLFEQPE
1010 1020 1030 1040 1050
FGHYTSIAKQ VLLALEQDNF CDFEIQYEIA HNYIHALVGG AQPYGMASLR
1060 1070 1080 1090 1100
YTAFDPLFYL HHSNTDRIWA IWQALQKYRG KPYNVANCAV TSMREPLQPF
1110 1120 1130 1140 1150
GLSANINTDH VTKEHSVPFN VFDYKTNFNY EYDTLEFNGL SISQLNKKLE
1160 1170 1180 1190 1200
AIKSQDRFFA GFLLSGFKKS SLVKFNICTD SSNCHPAGEF YLLGDENEMP
1210 1220 1230 1240 1250
WAYDRVFKYD ITEKLHDLKL HAEDHFYIDY EVFDLKPASL GKDLFKQPSV
1260 1270 1280 1290 1300
IHEPRIGHHE GEVYQAEVTS ANRIRKNIEN LSLGELESLR AAFLEIENDG
1310 1320 1330 1340 1350
TYESIAKFHG SPGLCQLNGN PISCCVHGMP TFPHWHRLYV VVVENALLKK
1360 1370 1380 1390 1400
GSSVAVPYWD WTKRIEHLPH LISDATYYNS RQHHYETNPF HHGKITHENE
1410 1420 1430 1440 1450
ITTRDPKDSL FHSDYFYEQV LYALEQDNFC DFEIQLEILH NALHSLLGGK
1460 1470 1480 1490 1500
GKYSMSNLDY AAFDPVFFLH HATTDRIWAI WQDLQRFRKR PYREANCAIQ
1510 1520 1530 1540 1550
LMHTPLQPFD KSDNNDEATK THATPHDGFE YQNSFGYAYD NLELNHYSIP
1560 1570 1580 1590 1600
QLDHMLQERK RHDRVFAGFL LHNIGTSADG HVFVCLPTGE HTKDCSHEAG
1610 1620 1630 1640 1650
MFSILGGQTE MSFVFDRLYK LDITKALKKN GVHLQGDFDL EIEITAVNGS
1660 1670 1680 1690 1700
HLDSHVIHSP TILFEAGTDS AHTDDGHTEP VMIRKDITQL DKRQQLSLVK
1710 1720 1730 1740 1750
ALESMKADHS SDGFQAIASF HALPPLCPSP AASKRFACCV HGMATFPQWH
1760 1770 1780 1790 1800
RLYTVQFQDS LRKHGAVVGL PYWDWTLPRS ELPELLTVST IHDPETGRDI
1810 1820 1830 1840 1850
PNPFIGSKIE FEGENVHTKR DINRDRLFQG STKTHHNWFI EQALLALEQT
1860 1870 1880 1890 1900
NYCDFEVQFE IMHNGVHTWV GGKEPYGIGH LHYASYDPLF YIHHSQTDRI
1910 1920 1930 1940 1950
WAIWQSLQRF RGLSGSEANC AVNLMKTPLK PFSFGAPYNL NDHTHDFSKP
1960 1970 1980 1990 2000
EDTFDYQKFG YIYDTLEFAG WSIRGIDHIV RNRQEHSRVF AGFLLEGFGT
2010 2020 2030 2040 2050
SATVDFQVCR TAGDCEDAGY FTVLGGEKEM PWAFDRLYKY DITETLDKMN
2060 2070 2080 2090 2100
LRHDEIFQIE VTITSYDGTV LDSGLIPTPS IIYDPAHHDI SSHHLSLNKV
2110 2120 2130 2140 2150
RHDLSTLSER DIGSLKYALS SLQADTSADG FAAIASFHGL PAKCNDSHNN
2160 2170 2180 2190 2200
EVACCIHGMP TFPHWHRLYT LQFEQALRRH GSSVAVPYWD WTKPIHNIPH
2210 2220 2230 2240 2250
LFTDKEYYDV WRNKVMPNPF ARGYVPSHDT YTVRDVQEGL FHLTSTGEHS
2260 2270 2280 2290 2300
ALLNQALLAL EQHDYCDFAV QFEVMHNTIH YLVGGPQVYS LSSLHYASYD
2310 2320 2330 2340 2350
PIFFIHHSFV DKVWAVWQAL QEKRGLPSDR ADCAVSLMTQ NMRPFHYEIN
2360 2370 2380 2390 2400
HNQFTKKHAV PNDVFKYELL GYRYDNLEIG GMNLHEIEKE IKDKQHHVRV
2410 2420 2430 2440 2450
FAGFLLHGIR TSADVQFQIC KTSEDCHHGG QIFVLGGTKE MAWAYNRLFK
2460 2470 2480 2490 2500
YDITHALHDA HITPEDVFHP SEPFFIKVSV TAVNGTVLPA SILHAPTIIY
2510 2520 2530 2540 2550
EPGLDHHEDH HSSSMAGHGV RKEINTLTTA EVDNLKDAMR AVMADHGPNG
2560 2570 2580 2590 2600
YQAIAAFHGN PPMCPMPDGK NYSCCTHGMA TFPHWHRLYT KQMEDALTAH
2610 2620 2630 2640 2650
GARVGLPYWD GTTAFTALPT FVTDEEDNPF HHGHIDYLGV DTTRSPRDKL
2660 2670 2680 2690 2700
FNDPERGSES FFYRQVLLAL EQTDFCQFEV QFEITHNAIH SWTGGLTPYG
2710 2720 2730 2740 2750
MSTLEYTTYD PLFWLHHANT DRIWAIWQAL QEYRGLPYDH ANCEIQAMKR
2760 2770 2780 2790 2800
PLRPFSDPIN HNAFTHSNAK PTDVFEYSRF NFQYDNLRFH GMTIKKLEHE
2810 2820 2830 2840 2850
LEKQKEEDRT FAAFLLHGIK KSADVSFDVC NHDGECHFAG TFAILGGEHE
2860 2870 2880 2890 2900
MPWSFDRLFR YDITQVLKQM HLEYDSDFTF HMRIIDTSGK QLPSDLIKMP
2910 2920 2930 2940 2950
TVEHSPGGKH HEKHHEDHHE DILVRKNIHS LSHHEAEELR DALYKLQNDE
2960 2970 2980 2990 3000
SHGGYEHIAG FHGYPNLCPE KGDEKYPCCV HGMSIFPHWH RLHTIQFERA
3010 3020 3030 3040 3050
LKKHGSHLGI PYWDWTQTIS SLPTFFADSG NNNPFFKYHI RSINQDTVRD
3060 3070 3080 3090 3100
VNEAIFQQTK FGEFSSIFYL ALQALEEDNY CDFEVQYEIL HNEVHALIGG
3110 3120 3130 3140 3150
AEKYSMSTLE YSAFDPYFMI HHASLDKIWI IWQELQKRRV KPAHAGSCAG
3160 3170 3180 3190 3200
DIMHVPLHPF NYESVNNDDF TRENSLPNAV VDSHRFNYKY DNLNLHGHNI
3210 3220 3230 3240 3250
EELEEVLRSL RLKSRVFAGF VLSGIRTTAV VKVYIKSGTD SDDEYAGSFV
3260 3270 3280 3290 3300
ILGGAKEMPW AYERLYRFDI TETVHNLNLT DDHVKFRFDL KKYDHTELDA
3310 3320 3330 3340 3350
SVLPAPIIVR RPNNAVFDII EIPIGKDVNL PPKVVVKRGT KIMFMSVDEA
3360 3370 3380 3390 3400
VTTPMLNLGS YTAMFKCKVP PFSFHAFELG KMYSVESGDY FMTASTTELC
3410
NDNNLRIHVH VDDE
Sequence cautioni
The sequence CAG28307 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAG28309 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 17 | E → G AA sequence (PubMed:8829804).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ698341 Genomic DNA Translation: CAG28309.2 Sequence problems. AJ698339 mRNA Translation: CAG28307.2 Sequence problems. |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ698341 Genomic DNA Translation: CAG28309.2 Sequence problems. AJ698339 mRNA Translation: CAG28307.2 Sequence problems. |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3L6W | X-ray | 4.00 | A/B | 2922-3412 | [»] | |
3QJO | X-ray | 4.00 | A/B | 2922-3412 | [»] | |
4BED | electron microscopy | 9.00 | A/C | 17-1680 | [»] | |
B/D | 1681-3414 | [»] | ||||
SMRi | Q10583 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
PTM databases
GlyConnecti | 211, 15 N-Linked glycans |
Family and domain databases
Gene3Di | 1.10.1280.10, 8 hits 2.60.310.10, 8 hits |
InterProi | View protein in InterPro IPR028999, Haemocyanin_beta-sandwich IPR036848, Haemocyanin_C_sf IPR002227, Tyrosinase_Cu-bd IPR008922, Unchr_di-copper_centre |
Pfami | View protein in Pfam PF14830, Haemocyan_bet_s, 8 hits PF00264, Tyrosinase, 9 hits |
PRINTSi | PR00092, TYROSINASE |
SUPFAMi | SSF48056, SSF48056, 8 hits SSF81277, SSF81277, 8 hits |
PROSITEi | View protein in PROSITE PS00497, TYROSINASE_1, 7 hits PS00498, TYROSINASE_2, 8 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | HCY1_MEGCR | |
Accessioni | Q10583Primary (citable) accession number: Q10583 Secondary accession number(s): Q53IP9, Q6KC56 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | June 17, 2020 | |
Last modified: | February 23, 2022 | |
This is version 60 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families