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Protein

Coagulation factor V

Gene

F5

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi139Calcium1
Metal bindingi140Calcium1
Metal bindingi1830Copper1
Metal bindingi1832Copper1
Metal bindingi1872Copper1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor
Cleaved into the following 2 chains:
Gene namesi
Name:F5
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000297429 – 2211Coagulation factor VAdd BLAST2183
ChainiPRO_000000297529 – 741Coagulation factor V heavy chainBy similarityAdd BLAST713
PropeptideiPRO_0000002976742 – 1564Activation peptide (connecting region)By similarityAdd BLAST823
ChainiPRO_00000029771565 – 2211Coagulation factor V light chainBy similarityAdd BLAST647

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi167 ↔ 193
Glycosylationi225N-linked (GlcNAc...)1 Publication1
Glycosylationi239N-linked (GlcNAc...)1 Publication1
Disulfide bondi248 ↔ 329
Glycosylationi297N-linked (GlcNAc...)Sequence analysis1
Glycosylationi382N-linked (GlcNAc...)Sequence analysis1
Glycosylationi460N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi499 ↔ 525
Glycosylationi553N-linked (GlcNAc...)Sequence analysis1
Glycosylationi587N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi607 ↔ 688
Modified residuei644PhosphothreonineBy similarity1
Modified residuei697SulfotyrosineSequence analysis1
Modified residuei701SulfotyrosineSequence analysis1
Modified residuei730SulfotyrosineSequence analysis1
Glycosylationi745N-linked (GlcNAc...)Sequence analysis1
Glycosylationi756N-linked (GlcNAc...)Sequence analysis1
Glycosylationi774N-linked (GlcNAc...)Sequence analysis1
Glycosylationi780N-linked (GlcNAc...)Sequence analysis1
Glycosylationi902N-linked (GlcNAc...)Sequence analysis1
Glycosylationi952N-linked (GlcNAc...)Sequence analysis1
Glycosylationi964N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1044N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1053N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1062N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1071N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1078N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1094N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1451N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1490N-linked (GlcNAc...)Sequence analysis1
Modified residuei1513SulfotyrosineSequence analysis1
Modified residuei1529SulfotyrosineSequence analysis1
Modified residuei1537SulfotyrosineSequence analysis1
Modified residuei1541SulfotyrosineSequence analysis1
Glycosylationi1550N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1690N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1712 ↔ 1738Curated
Glycosylationi1839N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1894 ↔ 2048
Glycosylationi1997N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2053 ↔ 2208
Glycosylationi2196N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus).
Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity.By similarity
Activated protein C inactivates factor V and factor Va by proteolytic degradation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei334 – 335Cleavage; by activated protein CBy similarity2
Sitei533 – 534Cleavage; by activated protein CBy similarity2
Sitei741 – 742Cleavage; by thrombinBy similarity2
Sitei1034 – 1035Cleavage; by thrombinBy similarity2
Sitei1564 – 1565Cleavage; by thrombin2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

PRIDEiQ28107.

Miscellaneous databases

PMAP-CutDBQ28107.

Interactioni

Subunit structurei

Factor Va, the activated form of factor V, is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. Forms heterodimer with SERPINA5 (By similarity).By similarity

Structurei

Secondary structure

12211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 43Combined sources7
Beta strandi61 – 67Combined sources7
Turni71 – 73Combined sources3
Beta strandi90 – 93Combined sources4
Beta strandi97 – 104Combined sources8
Beta strandi106 – 108Combined sources3
Beta strandi113 – 117Combined sources5
Turni121 – 123Combined sources3
Helixi134 – 137Combined sources4
Beta strandi147 – 153Combined sources7
Helixi156 – 158Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi166 – 173Combined sources8
Beta strandi176 – 178Combined sources3
Helixi179 – 183Combined sources5
Beta strandi188 – 193Combined sources6
Beta strandi202 – 207Combined sources6
Beta strandi217 – 219Combined sources3
Beta strandi222 – 225Combined sources4
Beta strandi230 – 232Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi262 – 264Combined sources3
Turni313 – 315Combined sources3
Helixi316 – 318Combined sources3
Beta strandi1570 – 1583Combined sources14
Turni1584 – 1587Combined sources4
Beta strandi1601 – 1612Combined sources12
Helixi1626 – 1628Combined sources3
Beta strandi1635 – 1638Combined sources4
Beta strandi1642 – 1647Combined sources6
Beta strandi1651 – 1653Combined sources3
Beta strandi1658 – 1660Combined sources3
Turni1701 – 1703Combined sources3
Beta strandi1707 – 1709Combined sources3
Beta strandi1711 – 1718Combined sources8
Helixi1723 – 1727Combined sources5
Turni1728 – 1730Combined sources3
Beta strandi1732 – 1738Combined sources7
Beta strandi1755 – 1764Combined sources10
Helixi1765 – 1767Combined sources3
Beta strandi1791 – 1795Combined sources5
Beta strandi1798 – 1800Combined sources3
Beta strandi1806 – 1808Combined sources3
Beta strandi1812 – 1819Combined sources8
Beta strandi1827 – 1831Combined sources5
Beta strandi1836 – 1838Combined sources3
Beta strandi1840 – 1842Combined sources3
Beta strandi1844 – 1851Combined sources8
Beta strandi1855 – 1862Combined sources8
Beta strandi1865 – 1872Combined sources8
Helixi1876 – 1879Combined sources4
Turni1880 – 1882Combined sources3
Beta strandi1884 – 1890Combined sources7
Turni1900 – 1902Combined sources3
Helixi1907 – 1909Combined sources3
Beta strandi1910 – 1913Combined sources4
Helixi1921 – 1923Combined sources3
Beta strandi1930 – 1932Combined sources3
Beta strandi1934 – 1936Combined sources3
Beta strandi1950 – 1966Combined sources17
Beta strandi1968 – 1990Combined sources23
Beta strandi1999 – 2002Combined sources4
Beta strandi2009 – 2013Combined sources5
Beta strandi2015 – 2038Combined sources24
Beta strandi2040 – 2048Combined sources9
Turni2059 – 2061Combined sources3
Beta strandi2062 – 2064Combined sources3
Beta strandi2069 – 2072Combined sources4
Turni2078 – 2080Combined sources3
Helixi2085 – 2087Combined sources3
Beta strandi2089 – 2091Combined sources3
Beta strandi2094 – 2096Combined sources3
Beta strandi2098 – 2100Combined sources3
Beta strandi2110 – 2126Combined sources17
Beta strandi2128 – 2130Combined sources3
Beta strandi2133 – 2140Combined sources8
Beta strandi2142 – 2149Combined sources8
Beta strandi2169 – 2172Combined sources4
Beta strandi2175 – 2190Combined sources16
Beta strandi2194 – 2198Combined sources5
Beta strandi2200 – 2208Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SDDX-ray2.80A29-334[»]
B1565-2211[»]
ProteinModelPortaliQ28107.
SMRiQ28107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28107.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 327F5/8 type A 1Add BLAST298
Domaini30 – 193Plastocyanin-like 1Add BLAST164
Domaini203 – 327Plastocyanin-like 2Add BLAST125
Domaini348 – 686F5/8 type A 2Add BLAST339
Domaini348 – 525Plastocyanin-like 3Add BLAST178
Domaini535 – 686Plastocyanin-like 4Add BLAST152
Repeati1124 – 11371-1Add BLAST14
Repeati1138 – 11511-2Add BLAST14
Repeati1188 – 11962-19
Repeati1197 – 12052-29
Repeati1206 – 12142-39
Repeati1215 – 12232-49
Repeati1224 – 12322-59
Repeati1233 – 12412-69
Repeati1242 – 12502-79
Repeati1251 – 12592-89
Repeati1260 – 12682-99
Repeati1269 – 12772-109
Repeati1278 – 12862-119
Repeati1287 – 12952-129
Repeati1296 – 13042-139
Repeati1305 – 13132-149
Repeati1314 – 13222-159
Repeati1323 – 13312-169
Repeati1332 – 13402-179
Repeati1341 – 13492-189
Repeati1350 – 13582-199
Repeati1359 – 13672-209
Repeati1368 – 13762-219
Repeati1377 – 13852-229
Repeati1386 – 13942-239
Repeati1395 – 14032-249
Repeati1404 – 14122-259
Repeati1413 – 14212-269
Repeati1422 – 14302-279
Repeati1431 – 14392-289
Repeati1440 – 14442-29; truncated5
Repeati1445 – 14532-309
Domaini1569 – 1890F5/8 type A 3Add BLAST322
Domaini1569 – 1738Plastocyanin-like 5Add BLAST170
Domaini1748 – 1890Plastocyanin-like 6Add BLAST143
Domaini1894 – 2048F5/8 type C 1PROSITE-ProRule annotationAdd BLAST155
Domaini2053 – 2208F5/8 type C 2PROSITE-ProRule annotationAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni696 – 1564BAdd BLAST869
Regioni1124 – 11512 X 14 AA tandem repeatsAdd BLAST28
Regioni1188 – 145330 X 9 AA approximate tandem repeats of [AS]-L-S-P-D-[LP]-[GS]-Q-[TE]Add BLAST266

Domaini

Domain B contains 29.5 X 9 AA tandem repeats, and 2 X 14 AA repeats.

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 F5/8 type A domains.Curated
Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
Contains 6 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000082542.
HOVERGENiHBG005631.
InParanoidiQ28107.
KOiK03902.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR009271. Coagulation_factor_V_LSPD.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR024715. Factor_5/8.
IPR029821. Factor_V.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF597. PTHR10127:SF597. 3 hits.
PfamiPF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
PF06049. LSPR. 28 hits.
[Graphical view]
PIRSFiPIRSF000354. Factors_V_VIII. 1 hit.
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q28107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLACPGFWV LVVLGSSWAG WGNLGAEAAK LRQFYVAAQS IRWNYRPEST
60 70 80 90 100
HLSSKPFETS FKKIVYREYE AYFQKEKPQS RTSGLLGPTL YAEVGDIMKV
110 120 130 140 150
HFKNKAHKPL SIHAQGIKYS KFSEGASYSD HTLPMEKMDD AVAPGQEYTY
160 170 180 190 200
EWIISEHSGP THDDPPCLTH IYYSYVNLVE DFNSGLIGPL LICKKGTLTE
210 220 230 240 250
DGTQKMFEKQ HVLMFAVFDE SKSWNQTSSL MYTVNGYVNG TMPDITVCAH
260 270 280 290 300
DHISWHLIGM SSGPELFSIH FNGQVLEQNH HKISAITLVS ATSTTANMTV
310 320 330 340 350
SPEGRWTIAS LIPRHFQAGM QAYIDIKNCA KKTRNPKKLT RDQRRHIKRW
360 370 380 390 400
EYFIAAEEVI WDYAPIIPAN MDKKYRSLHL DNFSNRIGKH YKKVVYKQYQ
410 420 430 440 450
DDSFTKRLED PSSEGDGILG PIIRAQVRDT LKIVFKNMAS RSYSIYPHGV
460 470 480 490 500
TFSPYDNEVN SSSTSGSNTM IRAVRPGETY TYKWNILESD EPTENDAQCL
510 520 530 540 550
TRPYYSNVDI TRDLASGLIG LLLICKSRSL DRRGIQRAAD IEQQAVFAVF
560 570 580 590 600
DENKSWYIED NIYKFCENPE KVKRDDPKFY ESNIMSNFTL PAINGYVPES
610 620 630 640 650
IPILGFCFDD TVQWHFCSVG TQNDILTIHF TGHSFIYGKR HEDTLTLFPM
660 670 680 690 700
QGESVTVTMD NVGTWMLTTM NSNPRSKKLR LRFRDAKCIR NDDDDSYEII
710 720 730 740 750
YEPSGSTAMT TKKIHDSSEI EDENDADSDY QDELALILGL RSFRNSSLNQ
760 770 780 790 800
EKDELNLTAL ALEKDSEFIP PSANRSLDSN SSSRSHVSRL IAKNFAESLK
810 820 830 840 850
TLLHLEAPAA GSPLEHAGLD KNSALNPPMA EHSSPYSEDP REDHPLSDVT
860 870 880 890 900
GVSLLPFGTG FKNRKPAKHQ RFQVGRGQAA KHKFSQTRFP AHKTRTRLSQ
910 920 930 940 950
DNSSSSRMGP WEDIPSDLLL LQQKDPYKIL NGEWHLVSEK GSYEIIQDAN
960 970 980 990 1000
ENKTVNKLPN SPQNDSRTWG ENIPFKNSHG KQSGHPTFLV TRRKPLQDRQ
1010 1020 1030 1040 1050
DRRNSRLKEG LPLIRTRRKK KEEKPAYHVP LSPRSFHPLR GEVNASFSDR
1060 1070 1080 1090 1100
RHNHSLLLHA SNETSLSIDL NQTFPSMNLS LAASLPDHDQ TSPNDTTSQT
1110 1120 1130 1140 1150
SSPPDLYPTV SPEEHYQIFP IQDSDPTHST TAPSNRSPDP THSTTAPSNR
1160 1170 1180 1190 1200
SPPTQPSQIP NYDLRNRAIP TDVSQIFPSL ELEVWQTATS LDLSQPSISP
1210 1220 1230 1240 1250
DLGQMALSPD PGQESLSPDL GQTSLSPDLS QESLSPDLGQ TALSPDPSQE
1260 1270 1280 1290 1300
SLSPDLGQTA LSPDPSQESL SPDLGQTALS PDPGQESLSP DLGQTSLSPD
1310 1320 1330 1340 1350
LSQESLSPDL GQTALSPDPS QESLSPDLGQ TALSPDPSQE SLSPDLGQTS
1360 1370 1380 1390 1400
LSPDLGQESL SPDLGQTALS PDPSQESLSP DLGQTSLSPD LGQESLSPDL
1410 1420 1430 1440 1450
GQTALSPDLS QESLSPDLGQ TPLSPDLSLE SLSPDLSQLD LKQTSPPLDL
1460 1470 1480 1490 1500
NQTSHTSESS QSLPLPEFGQ TFPNADIGQM PSPPPDSTLN NTFIPEEFNP
1510 1520 1530 1540 1550
LVVVGLSRDD GDYIEIIPRQ KEESSEEDYG EFEFVAYNDP YQTDLRTDIN
1560 1570 1580 1590 1600
SSRNPDNIAA WYLRSNTGNR KYYYIAAEEI SWDYSKFVQS DDVDYVPEDT
1610 1620 1630 1640 1650
VYKKVVFRKY LDSTFTKLDP QGEYEEHLGI LGPVIRAEVD DVIQVRFKNL
1660 1670 1680 1690 1700
ASRPYSLHAH GLSYEKSSEG KTYEDDSPEW FKEDNAIQPN KTYTYVWHAT
1710 1720 1730 1740 1750
TRSGPENPGS ACRAWAYYSA VNPEKDIHSG LIGPLLICRK GTLDKETNMP
1760 1770 1780 1790 1800
VDMREFVLLF MVFDEKKSWY YDKKPTRSWR RASSEVKNSH EFHAINGMIY
1810 1820 1830 1840 1850
NLPGLRMYEQ EWVRLHLLNL GGSRDIHVVH FHGQTLLENG TQQHQLGVWP
1860 1870 1880 1890 1900
LLPGSFKTLE MKASKPGWWL LDTEVGEIQR AGMQTPFLIV DRECKMPMGL
1910 1920 1930 1940 1950
STGLIADSQI QASEFWGYWE PKLARLNNGG SYNAWIAEKL STEFNPEPWI
1960 1970 1980 1990 2000
QVDMQKEVLL TGIQTQGAKH YLKPYYTTEF CVAYSLDRKN WRIFKGNSTR
2010 2020 2030 2040 2050
NVMYFGGNSD ASTIKENQID PPVVARYIRI SPTGSYNKPA LRLELQGCEV
2060 2070 2080 2090 2100
NGCSTPLGME SGKIENKQIT ASSFKKSWWG NYWEPFLARL NAQGRVNAWQ
2110 2120 2130 2140 2150
AKANNNNQWL QIDLLKIKKI TAIVTQGCKS LSSEMYVKSY TIHYSDQGTD
2160 2170 2180 2190 2200
WKPYREKSSM VDKIFEGNNN VRGHVKNFFN PPIISRFIRI IPKTWNQSIA
2210
LRLELFGCDM Y
Length:2,211
Mass (Da):248,983
Last modified:November 1, 1996 - v1
Checksum:iCBBF90B738667C45
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti587 – 592NFTLPA → T in variant 2. 6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81440 mRNA. Translation: AAA30512.1.
M81441 mRNA. Translation: AAA30513.1.
PIRiA42580. KFBO5.
RefSeqiNP_776304.1. NM_173879.2.
UniGeneiBt.23666.

Genome annotation databases

GeneIDi280687.
KEGGibta:280687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81440 mRNA. Translation: AAA30512.1.
M81441 mRNA. Translation: AAA30513.1.
PIRiA42580. KFBO5.
RefSeqiNP_776304.1. NM_173879.2.
UniGeneiBt.23666.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SDDX-ray2.80A29-334[»]
B1565-2211[»]
ProteinModelPortaliQ28107.
SMRiQ28107.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ28107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280687.
KEGGibta:280687.

Organism-specific databases

CTDi2153.

Phylogenomic databases

HOGENOMiHOG000082542.
HOVERGENiHBG005631.
InParanoidiQ28107.
KOiK03902.

Miscellaneous databases

EvolutionaryTraceiQ28107.
PMAP-CutDBQ28107.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR009271. Coagulation_factor_V_LSPD.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR024715. Factor_5/8.
IPR029821. Factor_V.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF597. PTHR10127:SF597. 3 hits.
PfamiPF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
PF06049. LSPR. 28 hits.
[Graphical view]
PIRSFiPIRSF000354. Factors_V_VIII. 1 hit.
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA5_BOVIN
AccessioniPrimary (citable) accession number: Q28107
Secondary accession number(s): Q28108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.