UniProtKB - P07897 (PGCA_RAT)
Aggrecan core protein
Acan
Functioni
This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1975 | Calcium 1 | 1 | |
Metal bindingi | 1979 | Calcium 1 | 1 | |
Metal bindingi | 1979 | Calcium 3 | 1 | |
Metal bindingi | 1999 | Calcium 2 | 1 | |
Metal bindingi | 2001 | Calcium 2 | 1 | |
Metal bindingi | 2002 | Calcium 1 | 1 | |
Metal bindingi | 2008 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 2008 | Calcium 2 | 1 | |
Metal bindingi | 2009 | Calcium 1 | 1 | |
Metal bindingi | 2009 | Calcium 3 | 1 | |
Metal bindingi | 2022 | Calcium 2 | 1 | |
Metal bindingi | 2023 | Calcium 2 | 1 | |
Metal bindingi | 2023 | Calcium 2; via carbonyl oxygen | 1 |
GO - Molecular functioni
- calcium ion binding Source: RGD
- carbohydrate binding Source: UniProtKB-KW
- hyaluronic acid binding Source: InterPro
GO - Biological processi
- cartilage condensation Source: RGD
- cell adhesion Source: InterPro
- cellular response to growth factor stimulus Source: RGD
- central nervous system development Source: RGD
- chondroblast differentiation Source: RGD
- chondrocyte development Source: RGD
- collagen fibril organization Source: RGD
- heart development Source: RGD
- multicellular organism aging Source: RGD
- negative regulation of cell migration Source: RGD
- ossification Source: RGD
- proteoglycan biosynthetic process Source: RGD
- response to acidic pH Source: RGD
- response to glucose Source: RGD
- response to gravity Source: RGD
- response to mechanical stimulus Source: RGD
- response to organic cyclic compound Source: RGD
- response to radiation Source: RGD
- response to xenobiotic stimulus Source: RGD
- skeletal system development Source: GO_Central
- spinal cord development Source: RGD
Keywordsi
Ligand | Lectin, Metal-binding |
Enzyme and pathway databases
Reactomei | R-RNO-1474228, Degradation of the extracellular matrix R-RNO-2022854, Keratan sulfate biosynthesis R-RNO-2022857, Keratan sulfate degradation R-RNO-3000178, ECM proteoglycans |
Names & Taxonomyi
Protein namesi | Recommended name: Aggrecan core proteinAlternative name(s): Cartilage-specific proteoglycan core protein Short name: CSPCP |
Gene namesi | Name:Acan Synonyms:Agc, Agc1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 68358, Acan |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix By similarity
Extracellular region or secreted
- extracellular space Source: RGD
Other locations
- basement membrane Source: RGD
- extracellular matrix Source: RGD
- GABA-ergic synapse Source: RGD
- glutamatergic synapse Source: RGD
- neuron projection Source: RGD
- neuronal cell body Source: RGD
- perineuronal net Source: RGD
- perisynaptic extracellular matrix Source: RGD
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 19 | 1 PublicationAdd BLAST | 19 | |
ChainiPRO_0000017508 | 20 – 2124 | Aggrecan core proteinAdd BLAST | 2105 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 51 ↔ 133 | By similarity | ||
Glycosylationi | 126 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 175 ↔ 246 | By similarity | ||
Disulfide bondi | 199 ↔ 220 | By similarity | ||
Glycosylationi | 239 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 273 ↔ 348 | By similarity | ||
Disulfide bondi | 297 ↔ 318 | By similarity | ||
Glycosylationi | 333 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 371 | O-linked (Xyl...) (keratan sulfate) threonineBy similarity | 1 | |
Glycosylationi | 376 | O-linked (Xyl...) (keratan sulfate) threonineBy similarity | 1 | |
Glycosylationi | 387 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 509 ↔ 580 | By similarity | ||
Disulfide bondi | 533 ↔ 554 | By similarity | ||
Disulfide bondi | 607 ↔ 682 | By similarity | ||
Glycosylationi | 611 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 631 ↔ 652 | By similarity | ||
Glycosylationi | 667 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1842 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1914 ↔ 1925 | By similarity | ||
Disulfide bondi | 1942 ↔ 2034 | 1 Publication | ||
Disulfide bondi | 2010 ↔ 2026 | 1 Publication | ||
Disulfide bondi | 2041 ↔ 2084 | By similarity | ||
Disulfide bondi | 2070 ↔ 2097 | By similarity |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, ProteoglycanProteomic databases
PaxDbi | P07897 |
PTM databases
GlyGeni | P07897, 9 sites |
iPTMneti | P07897 |
Interactioni
Subunit structurei
Interacts with FBLN1 and COMP.
By similarityProtein-protein interaction databases
BioGRIDi | 248701, 1 interactor |
IntActi | P07897, 2 interactors |
MINTi | P07897 |
STRINGi | 10116.ENSRNOP00000042691 |
Structurei
Secondary structure
3D structure databases
SMRi | P07897 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07897 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 34 – 147 | Ig-like V-typeAdd BLAST | 114 | |
Domaini | 153 – 248 | Link 1PROSITE-ProRule annotationAdd BLAST | 96 | |
Domaini | 254 – 350 | Link 2PROSITE-ProRule annotationAdd BLAST | 97 | |
Domaini | 487 – 582 | Link 3PROSITE-ProRule annotationAdd BLAST | 96 | |
Domaini | 588 – 684 | Link 4PROSITE-ProRule annotationAdd BLAST | 97 | |
Domaini | 1910 – 2036 | C-type lectinPROSITE-ProRule annotationAdd BLAST | 127 | |
Domaini | 2039 – 2099 | SushiPROSITE-ProRule annotationAdd BLAST | 61 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 48 – 140 | G1-AAdd BLAST | 93 | |
Regioni | 152 – 247 | G1-BAdd BLAST | 96 | |
Regioni | 253 – 349 | G1-B'Add BLAST | 97 | |
Regioni | 434 – 454 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 486 – 580 | G2-BAdd BLAST | 95 | |
Regioni | 587 – 682 | G2-B'Add BLAST | 96 | |
Regioni | 685 – 798 | KSAdd BLAST | 114 | |
Regioni | 731 – 1042 | DisorderedSequence analysisAdd BLAST | 312 | |
Regioni | 801 – 1226 | CS-1Add BLAST | 426 | |
Regioni | 1100 – 1212 | DisorderedSequence analysisAdd BLAST | 113 | |
Regioni | 1225 – 1253 | DisorderedSequence analysisAdd BLAST | 29 | |
Regioni | 1227 – 1909 | CS-2Add BLAST | 683 | |
Regioni | 1295 – 1455 | DisorderedSequence analysisAdd BLAST | 161 | |
Regioni | 1579 – 1661 | DisorderedSequence analysisAdd BLAST | 83 | |
Regioni | 1723 – 1913 | DisorderedSequence analysisAdd BLAST | 191 | |
Regioni | 1910 – 2124 | G3Add BLAST | 215 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 768 – 885 | Polar residuesSequence analysisAdd BLAST | 118 | |
Compositional biasi | 892 – 924 | Polar residuesSequence analysisAdd BLAST | 33 | |
Compositional biasi | 970 – 1002 | Polar residuesSequence analysisAdd BLAST | 33 | |
Compositional biasi | 1009 – 1023 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1108 – 1122 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1318 – 1455 | Polar residuesSequence analysisAdd BLAST | 138 | |
Compositional biasi | 1602 – 1661 | Polar residuesSequence analysisAdd BLAST | 60 | |
Compositional biasi | 1766 – 1789 | Polar residuesSequence analysisAdd BLAST | 24 | |
Compositional biasi | 1797 – 1913 | Polar residuesSequence analysisAdd BLAST | 117 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Immunoglobulin domain, Repeat, Signal, SushiPhylogenomic databases
eggNOGi | ENOG502QUX8, Eukaryota |
InParanoidi | P07897 |
OrthoDBi | 156064at2759 |
Family and domain databases
CDDi | cd00033, CCP, 1 hit cd03588, CLECT_CSPGs, 1 hit |
Gene3Di | 2.60.40.10, 1 hit 3.10.100.10, 5 hits |
InterProi | View protein in InterPro IPR001304, C-type_lectin-like IPR016186, C-type_lectin-like/link_sf IPR018378, C-type_lectin_CS IPR033987, CSPG_CTLD IPR016187, CTDL_fold IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR003006, Ig/MHC_CS IPR003599, Ig_sub IPR013106, Ig_V-set IPR000538, Link_dom IPR035976, Sushi/SCR/CCP_sf IPR000436, Sushi_SCR_CCP_dom |
Pfami | View protein in Pfam PF00059, Lectin_C, 1 hit PF00084, Sushi, 1 hit PF07686, V-set, 1 hit PF00193, Xlink, 4 hits |
PRINTSi | PR01265, LINKMODULE |
SMARTi | View protein in SMART SM00032, CCP, 1 hit SM00034, CLECT, 1 hit SM00409, IG, 1 hit SM00406, IGv, 1 hit SM00445, LINK, 4 hits |
SUPFAMi | SSF48726, SSF48726, 1 hit SSF56436, SSF56436, 5 hits SSF57535, SSF57535, 1 hit |
PROSITEi | View protein in PROSITE PS00615, C_TYPE_LECTIN_1, 1 hit PS50041, C_TYPE_LECTIN_2, 1 hit PS50835, IG_LIKE, 1 hit PS00290, IG_MHC, 1 hit PS01241, LINK_1, 4 hits PS50963, LINK_2, 4 hits PS50923, SUSHI, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MTTLLLVFVT LRVIAAVISE EVPDHDNSLS VSIPQPSPLK ALLGTSLTIP
60 70 80 90 100
CYFIDPMHPV TTAPSTAPLT PRIKWSRVSK EKEVVLLVAT EGQVRVNSIY
110 120 130 140 150
QDKVSLPNYP AIPSDATLEI QNLRSNDSGI YRCEVMHGIE DSEATLEVIV
160 170 180 190 200
KGIVFHYRAI STRYTLDFDR AQRACLQNSA IIATPEQLQA AYEDGFHQCD
210 220 230 240 250
AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE TYDVYCFAEE
260 270 280 290 300
MEGEVFYATS PEKFTFQEAA NECRTVGARL ATTGQLYLAW QGGMDMCSAG
310 320 330 340 350
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT
360 370 380 390 400
GEDFVDIPEN FFGVGGEEDI TIQTVTWPDL ELPLPRNITE GEARGNVILT
410 420 430 440 450
AKPIFDMSPT VSEPGEALTL APEVGTTVFP EAGERTEKTT RPWGFPEEAT
460 470 480 490 500
RGPDSATAFA SEDLVVRVTI SPGAVEVPGQ PRLPGGVVFH YRPGSTRYSL
510 520 530 540 550
TFEEAQQACI RTGAAIASPE QLQAAYEAGY EQCDAGWLQD QTVRYPIVSP
560 570 580 590 600
RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATQMEQFTF
610 620 630 640 650
QEAQAFCAAQ NATLASTGQL YAAWSQGLDK CYAGWLADGT LRYPIVNPRP
660 670 680 690 700
ACGGDKPGVR TVYLYPNQTG LPDPLSKHHA FCFRGVSVVP SPGGTPTSPS
710 720 730 740 750
DIEDWIVTRV EPGVDAVPLE PETTEVPYFT TEPEKQTEWE PAYTPVGTSP
760 770 780 790 800
LPGIPPTWLP TVPAAEEHTE SPSASQEPSA SQVPSTSEEP YTPSLAVPSG
810 820 830 840 850
TELPSSGDTS GAPDLSGDFT GSTDTSGRLD SSGEPSGGSE SGLPSGDLDS
860 870 880 890 900
SGLGPTVSSG LPVESGSASG DGEIPWSSTP TVDRLPSGGE SLEGSASASG
910 920 930 940 950
TGDLSGLPSG GEITETSASG TEEISGLPSG GDDLETSTSG IDGASVLPTG
960 970 980 990 1000
RGGLETSASG VEDLSGLPSG EEGSETSTSG IEDISVLPTG ESPETSASGV
1010 1020 1030 1040 1050
GDLSGLPSGG ESLETSASGV EDVTQLPTER GGLETSASGI EDITVLPTGR
1060 1070 1080 1090 1100
ENLETSASGV EDVSGLPSGK EGLETSASGI EDISVFPTEA EGLETSASGG
1110 1120 1130 1140 1150
YVSGIPSGED GTETSTSGVE GVSGLPSGGE GLETSASGVE DLGLPTRDSL
1160 1170 1180 1190 1200
ETSASGVDVT GYPSGREDTE TSVPGVGDDL SGLPSGQEGL ETSASGAEDL
1210 1220 1230 1240 1250
GGLPSGKEDL VGSASGALDF GKLPSGTLGS GQTPEASGLP SGFSGEYSGV
1260 1270 1280 1290 1300
DIGSGPSSGL PDFSGLPSGF PTVSLVDSTL VEVITATTAS ELEGRGTISV
1310 1320 1330 1340 1350
SGSGEESGPP LSELDSSADI SGLPSGTELS GQTSGSLDVS GETSGFFDVS
1360 1370 1380 1390 1400
GQPFGSSGTG EGTSGIPEVS GQAVRSPDTT EISELSGLSS GQPDVSGEGS
1410 1420 1430 1440 1450
GILFGSGQSS GITSVSGETS GISDLSGQPS GFPVLSGTTP GTPDLASGAM
1460 1470 1480 1490 1500
SGSGDSSGIT FVDTSLIEVT PTTFREEEGL GSVELSGLPS GETDLSGTSG
1510 1520 1530 1540 1550
MVDVSGQSSG AIDSSGLISP TPEFSGLPSG VAEVSGEVSG VETGSSLSSG
1560 1570 1580 1590 1600
AFDGSGLVSG FPTVSLVDRT LVESITLAPT AQEAGEGPSS ILEFSGAHSG
1610 1620 1630 1640 1650
TPDISGDLSG SLDQSTWQPG WTEASTEPPS SPYFSGDFSS TTDASGESIT
1660 1670 1680 1690 1700
APTGSGETSG LPEVTLITSE LVEGVTEPTV SQELGHGPSM TYTPRLFEAS
1710 1720 1730 1740 1750
GEASASGDLG GPVTIFPGSG VEASVPEGSS DPSAYPEAGV GVSAAPEASS
1760 1770 1780 1790 1800
QLSEFPDLHG ITSASRETDL EMTTPGTEVS SNPWTFQEGT REGSAAPEVS
1810 1820 1830 1840 1850
GESSTTSDID AGTSGVPFAT PMTSGDRTEI SGEWSDHTSE VNVTVSTTVP
1860 1870 1880 1890 1900
ESRWAQSTQH PTETLQEIGS PNPSYSGEET QTAETAKSLT DTPTLASPEG
1910 1920 1930 1940 1950
SGETESTAAD QEQCEEGWTK FQGHCYRHFP DRETWVDAER RCREQQSHLS
1960 1970 1980 1990 2000
SIVTPEEQEF VNKNAQDYQW IGLNDRTIEG DFRWSDGHSL QFEKWRPNQP
2010 2020 2030 2040 2050
DNFFATGEDC VVMIWHERGE WNDVPCNYQL PFTCKKGTVA CGEPPAVEHA
2060 2070 2080 2090 2100
RTLGQKKDRY EISSLVRYQC TEGFVQRHVP TIRCQPSADW EEPRITCTDP
2110 2120
NTYKHRLQKR TMRPTRRSRP SMAH
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketD4A7Y1 | D4A7Y1_RAT | Aggrecan core protein | Acan | 2,162 | Annotation score: | ||
F1LQI4 | F1LQI4_RAT | Aggrecan core protein | Acan | 2,121 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 38 | P → W AA sequence (PubMed:3693371).Curated | 1 | |
Sequence conflicti | 61 | T → E AA sequence (PubMed:3693371).Curated | 1 | |
Sequence conflicti | 149 | I → L AA sequence (PubMed:3693371).Curated | 1 | |
Sequence conflicti | 239 | N → S AA sequence (PubMed:3693371).Curated | 1 | |
Sequence conflicti | 241 | T → A AA sequence (PubMed:3693371).Curated | 1 | |
Sequence conflicti | 275 – 276 | TV → RL in AAA21000 (PubMed:3693370).Curated | 2 | |
Sequence conflicti | 374 | T → H AA sequence (PubMed:3693371).Curated | 1 | |
Sequence conflicti | 377 | W → E AA sequence (PubMed:3693371).Curated | 1 | |
Sequence conflicti | 380 | L → V AA sequence (PubMed:3693371).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_039196 | 1909 | A → ADIDECLSSPCLNGATCVDA LDTFTCLCLPSYRGDLCEI in isoform 2. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03485 mRNA Translation: AAA21000.1 M13518 mRNA Translation: AAA41836.1 |
PIRi | A92623, A28452 |
RefSeqi | NP_071526.1, NM_022190.1 |
Genome annotation databases
GeneIDi | 58968 |
UCSCi | RGD:68358, rat [P07897-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03485 mRNA Translation: AAA21000.1 M13518 mRNA Translation: AAA41836.1 |
PIRi | A92623, A28452 |
RefSeqi | NP_071526.1, NM_022190.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1TDQ | X-ray | 2.60 | B | 1909-2037 | [»] | |
SMRi | P07897 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 248701, 1 interactor |
IntActi | P07897, 2 interactors |
MINTi | P07897 |
STRINGi | 10116.ENSRNOP00000042691 |
PTM databases
GlyGeni | P07897, 9 sites |
iPTMneti | P07897 |
Proteomic databases
PaxDbi | P07897 |
Genome annotation databases
GeneIDi | 58968 |
UCSCi | RGD:68358, rat [P07897-1] |
Organism-specific databases
CTDi | 176 |
RGDi | 68358, Acan |
Phylogenomic databases
eggNOGi | ENOG502QUX8, Eukaryota |
InParanoidi | P07897 |
OrthoDBi | 156064at2759 |
Enzyme and pathway databases
Reactomei | R-RNO-1474228, Degradation of the extracellular matrix R-RNO-2022854, Keratan sulfate biosynthesis R-RNO-2022857, Keratan sulfate degradation R-RNO-3000178, ECM proteoglycans |
Miscellaneous databases
EvolutionaryTracei | P07897 |
PROi | PR:P07897 |
Family and domain databases
CDDi | cd00033, CCP, 1 hit cd03588, CLECT_CSPGs, 1 hit |
Gene3Di | 2.60.40.10, 1 hit 3.10.100.10, 5 hits |
InterProi | View protein in InterPro IPR001304, C-type_lectin-like IPR016186, C-type_lectin-like/link_sf IPR018378, C-type_lectin_CS IPR033987, CSPG_CTLD IPR016187, CTDL_fold IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR003006, Ig/MHC_CS IPR003599, Ig_sub IPR013106, Ig_V-set IPR000538, Link_dom IPR035976, Sushi/SCR/CCP_sf IPR000436, Sushi_SCR_CCP_dom |
Pfami | View protein in Pfam PF00059, Lectin_C, 1 hit PF00084, Sushi, 1 hit PF07686, V-set, 1 hit PF00193, Xlink, 4 hits |
PRINTSi | PR01265, LINKMODULE |
SMARTi | View protein in SMART SM00032, CCP, 1 hit SM00034, CLECT, 1 hit SM00409, IG, 1 hit SM00406, IGv, 1 hit SM00445, LINK, 4 hits |
SUPFAMi | SSF48726, SSF48726, 1 hit SSF56436, SSF56436, 5 hits SSF57535, SSF57535, 1 hit |
PROSITEi | View protein in PROSITE PS00615, C_TYPE_LECTIN_1, 1 hit PS50041, C_TYPE_LECTIN_2, 1 hit PS50835, IG_LIKE, 1 hit PS00290, IG_MHC, 1 hit PS01241, LINK_1, 4 hits PS50963, LINK_2, 4 hits PS50923, SUSHI, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PGCA_RAT | |
Accessioni | P07897Primary (citable) accession number: P07897 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | July 1, 1989 | |
Last modified: | February 23, 2022 | |
This is version 173 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families