Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Patatin-like phospholipase domain-containing protein 7

Gene

Pnpla7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine hydrolase, whose specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy (By similarity). Isoform 1 and isoform 2 have equal enzyme activity. Isoform 3 has no enzyme activity.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei983 – 9831By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi170 – 297128cNMP 1Add
BLAST
Nucleotide bindingi478 – 602125cNMP 2Add
BLAST
Nucleotide bindingi598 – 718121cNMP 3Add
BLAST

GO - Molecular functioni

  • lysophospholipase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiR-MMU-6814848. Glycerophospholipid catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Patatin-like phospholipase domain-containing protein 7 (EC:3.1.1.-)
Alternative name(s):
Neuropathy target esterase-related esterase
Short name:
NRE
Short name:
NTE-related esterase
Gene namesi
Name:Pnpla7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2385325. Pnpla7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei37 – 5721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lysosome, Membrane, Microsome, Mitochondrion, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3259499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13521352Patatin-like phospholipase domain-containing protein 7PRO_0000293490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence analysis
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei379 – 3791PhosphoserineBy similarity
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence analysis
Glycosylationi750 – 7501N-linked (GlcNAc...)Sequence analysis
Glycosylationi1036 – 10361N-linked (GlcNAc...)Sequence analysis
Glycosylationi1255 – 12551N-linked (GlcNAc...)Sequence analysis
Modified residuei1280 – 12801PhosphoserineCombined sources
Modified residuei1284 – 12841PhosphothreonineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiA2AJ88.
MaxQBiA2AJ88.
PaxDbiA2AJ88.
PRIDEiA2AJ88.

PTM databases

iPTMnetiA2AJ88.
PhosphoSiteiA2AJ88.

Expressioni

Tissue specificityi

Isoform 1, isoform 2 and isoform 3 are expressed in white adipose tissue, cardiac muscle, skeletal muscle, and testis.1 Publication

Inductioni

By nutritional conditions. Expression of isoform 3 is switched to the expression of isoform 2 during fasting. In the examined tissues, high expression levels of isoform 3 are detected in fed status, but expression is significantly decreased to about one fourth in fasted status. Isoform 2 expression levels are down-regulated under fed status and are up-regulated in fasted status. Isoform 1 expression levels are not affected by fasting.1 Publication

Gene expression databases

BgeeiA2AJ88.
CleanExiMM_PNPLA7.
ExpressionAtlasiA2AJ88. baseline and differential.
GenevisibleiA2AJ88. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000044078.

Structurei

3D structure databases

ProteinModelPortaliA2AJ88.
SMRiA2AJ88. Positions 469-692.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini950 – 1116167PatatinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi981 – 9855GXSXG

Sequence similaritiesi

Belongs to the NTE family.Curated
Contains 3 cyclic nucleotide-binding domains.PROSITE-ProRule annotation
Contains 1 patatin domain.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2968. Eukaryota.
COG0664. LUCA.
COG1752. LUCA.
GeneTreeiENSGT00390000002533.
HOVERGENiHBG053067.
InParanoidiA2AJ88.
KOiK14676.
OMAiCAQVGIL.
OrthoDBiEOG7QRQT1.
PhylomeDBiA2AJ88.
TreeFamiTF300519.

Family and domain databases

Gene3Di2.60.120.10. 3 hits.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR002641. Patatin/PLipase_A2-rel.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 3 hits.
PF01734. Patatin. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 3 hits.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 3 hits.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A2AJ88-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQNEEDACLE AGYCLGTTLS SWRLHFMEEQ SQSTMLMGIG IGALLTLAFV
60 70 80 90 100
GITFFFVYRR VRRLRRAEPT PQYRFRKRDK VMFYGRKIMR KVTTLPHTLV
110 120 130 140 150
GNTSAPRQRV RKRTKVLSLA KRILRFKKEY PTLQPKEPPP SLLEADLTEF
160 170 180 190 200
DVKNSHLPSE VLYMLKNVRV LGHFEKPLFL ELCKHMVFVQ LQEGEHVFQP
210 220 230 240 250
GEPDISIYVV QDGRLEVCIQ DADGTEVVVK EVLPGDSVHS LLSILDVITG
260 270 280 290 300
HTAPYKTVSA RAAVSSTVLW LPAAAFQGVF EKYPETLVRV VQIIMVRLQR
310 320 330 340 350
VTFLALHNYL GLTTELFNPE SQAIPLLSVA SVAGRAKRQM SYGPEEQLER
360 370 380 390 400
SLRPSEFSSS DHGSSCVTVS GPLLKRSCSV PLPSNHGEVD ELRQSQGSGS
410 420 430 440 450
NTSAFQESHE GATSDLGMAY NRARILPHSD EQLGNSLASK SKKSVVAETP
460 470 480 490 500
SAIFHYSENF RDETGACGKT DAIFRAATKD LLTLMKLDDP SLLDGRVAFL
510 520 530 540 550
HVPAGTLVSK QGDQDVNILF VVSGMLHVYQ QKIDSLEDTC LFLTHPGEMV
560 570 580 590 600
GQLAVLTGEP LMFTIRANRD CSFLSISKAH FYEIMRKRPD VVLGVAHTVV
610 620 630 640 650
KRMSSFVRQI DFALDWMEVE AGRAIYRQGD KSDCTYIVLS GRLRSVIRKD
660 670 680 690 700
DGKKRLAGEY GRGDLVGVVE TLTHQARATT VHAVRDSELA KLPAGALTSI
710 720 730 740 750
KRRYPQVVTR LIHLLGEKIL GSLQQGSATG HQLGFNTASS KWDLGNPPGN
760 770 780 790 800
LSTVAALPAS EDVPLTAFAL ELQHALSAIG PVLLLTSDNI KQRLGSAALD
810 820 830 840 850
SIHEYRLSSW LGQQEDIHRI VLYQADGTLT PWTQRCIRQA DCILIVGLGE
860 870 880 890 900
QEPAVGELEQ MLESTAVRAQ KQLILLHKED GPVPSRTVEW LNMRSWCSGH
910 920 930 940 950
LHLCCPRRVF SKRSLPKLVE MYTRVFQRPP DRHSDFSRLA RMLTGNAIAL
960 970 980 990 1000
VLGGGGARGC AQVGILRALA ECGVPVDIIG GTSIGAFMGA LFAEERSYSQ
1010 1020 1030 1040 1050
TRIRAKQWAE GMTSMMKTIL DLTYPITSMF SGTGFNSSIS NIFKDRQIED
1060 1070 1080 1090 1100
LWLPYFAITT DITASAMRVH TDGSLWRYVR ASMSLSGYMP PLCDPKDGHL
1110 1120 1130 1140 1150
LMDGGYINNL PADVARSMGA KVVIAIDVGS RDETDLTNYG DALSGWWLLW
1160 1170 1180 1190 1200
KRWNPLATKV KVLNMAEIQT RLAYVCCVRQ LEMVKNSDYC EYLRPPIDSY
1210 1220 1230 1240 1250
RTLDFGKFDE ICEVGYQHGR TVFDIWVRSG VLEKMLQDQQ GTSKRKDCGV
1260 1270 1280 1290 1300
FTCPNSSFTD LAEIVSRIEP AKVAAVDDES DYQTEYEEEL PAIPKETYAD
1310 1320 1330 1340 1350
FQSTGIELDS DSEYEPSMLQ GPPSLTSPEQ SQDSFPWLPN QDDQGPRLEH

PS
Length:1,352
Mass (Da):150,494
Last modified:February 20, 2007 - v1
Checksum:iADF5362282EA1607
GO
Isoform 2 (identifier: A2AJ88-2) [UniParc]FASTAAdd to basket

Also known as: mNREV1

The sequence of this isoform differs from the canonical sequence as follows:
     1313-1326: EYEPSMLQGPPSLT → VRNMSLRCCKDPPA
     1327-1352: Missing.

Show »
Length:1,326
Mass (Da):147,561
Checksum:i69C4D7B64211DA35
GO
Isoform 3 (identifier: A2AJ88-3) [UniParc]FASTAAdd to basket

Also known as: mNREV2

The sequence of this isoform differs from the canonical sequence as follows:
     780-833: GPVLLLTSDN...QADGTLTPWT → ASMSTGSPVG...SWAWVSKSQQ
     834-1352: Missing.

Show »
Length:833
Mass (Da):91,942
Checksum:iBB7939ED3A7920DC
GO

Sequence cautioni

The sequence AAH27342.1 differs from that shown.Intron retention.Curated
The sequence AAH27342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI41366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI41367.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC40302.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE28519.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE41783.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1164RTKV → PRVR in AAH25621 (PubMed:15489334).Curated
Sequence conflicti237 – 2371S → R in BAE41783 (PubMed:16141072).Curated
Sequence conflicti604 – 6041S → P in ABX89593 (PubMed:22326266).Curated
Sequence conflicti604 – 6041S → P in ABY82074 (PubMed:22326266).Curated
Sequence conflicti604 – 6041S → P in ABY89725 (PubMed:22326266).Curated
Sequence conflicti1343 – 13431D → N in BAE28519 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei780 – 83354GPVLL…LTPWT → ASMSTGSPVGWASRRTSNGL CCIRQTAHSHRGPSAASGRL TASSSWAWVSKSQQ in isoform 3. 1 PublicationVSP_053967Add
BLAST
Alternative sequencei834 – 1352519Missing in isoform 3. 1 PublicationVSP_053968Add
BLAST
Alternative sequencei1313 – 132614EYEPS…PPSLT → VRNMSLRCCKDPPA in isoform 2. 2 PublicationsVSP_026506Add
BLAST
Alternative sequencei1327 – 135226Missing in isoform 2. 2 PublicationsVSP_026507Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088362 mRNA. Translation: BAC40302.1. Different initiation.
AK148380 mRNA. Translation: BAE28519.1. Different initiation.
AK170417 mRNA. Translation: BAE41783.1. Different initiation.
AL732585 Genomic DNA. No translation available.
BC025621 mRNA. Translation: AAH25621.1.
BC027342 mRNA. Translation: AAH27342.1. Sequence problems.
BC064003 mRNA. Translation: AAH64003.1.
BC080793 mRNA. Translation: AAH80793.1.
BC141365 mRNA. Translation: AAI41366.1. Different initiation.
BC141366 mRNA. Translation: AAI41367.1. Different initiation.
EU293208 mRNA. Translation: ABX89593.1.
EU368675 mRNA. Translation: ABY82074.1.
EU402948 mRNA. Translation: ABY89725.2.
CCDSiCCDS50522.1. [A2AJ88-1]
RefSeqiNP_666363.3. NM_146251.4. [A2AJ88-1]
UniGeneiMm.389243.

Genome annotation databases

EnsembliENSMUST00000045295; ENSMUSP00000044078; ENSMUSG00000036833. [A2AJ88-1]
GeneIDi241274.
KEGGimmu:241274.
UCSCiuc008ipv.2. mouse. [A2AJ88-1]
uc012brs.1. mouse. [A2AJ88-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088362 mRNA. Translation: BAC40302.1. Different initiation.
AK148380 mRNA. Translation: BAE28519.1. Different initiation.
AK170417 mRNA. Translation: BAE41783.1. Different initiation.
AL732585 Genomic DNA. No translation available.
BC025621 mRNA. Translation: AAH25621.1.
BC027342 mRNA. Translation: AAH27342.1. Sequence problems.
BC064003 mRNA. Translation: AAH64003.1.
BC080793 mRNA. Translation: AAH80793.1.
BC141365 mRNA. Translation: AAI41366.1. Different initiation.
BC141366 mRNA. Translation: AAI41367.1. Different initiation.
EU293208 mRNA. Translation: ABX89593.1.
EU368675 mRNA. Translation: ABY82074.1.
EU402948 mRNA. Translation: ABY89725.2.
CCDSiCCDS50522.1. [A2AJ88-1]
RefSeqiNP_666363.3. NM_146251.4. [A2AJ88-1]
UniGeneiMm.389243.

3D structure databases

ProteinModelPortaliA2AJ88.
SMRiA2AJ88. Positions 469-692.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000044078.

Chemistry

ChEMBLiCHEMBL3259499.

PTM databases

iPTMnetiA2AJ88.
PhosphoSiteiA2AJ88.

Proteomic databases

EPDiA2AJ88.
MaxQBiA2AJ88.
PaxDbiA2AJ88.
PRIDEiA2AJ88.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045295; ENSMUSP00000044078; ENSMUSG00000036833. [A2AJ88-1]
GeneIDi241274.
KEGGimmu:241274.
UCSCiuc008ipv.2. mouse. [A2AJ88-1]
uc012brs.1. mouse. [A2AJ88-2]

Organism-specific databases

CTDi375775.
MGIiMGI:2385325. Pnpla7.

Phylogenomic databases

eggNOGiKOG2968. Eukaryota.
COG0664. LUCA.
COG1752. LUCA.
GeneTreeiENSGT00390000002533.
HOVERGENiHBG053067.
InParanoidiA2AJ88.
KOiK14676.
OMAiCAQVGIL.
OrthoDBiEOG7QRQT1.
PhylomeDBiA2AJ88.
TreeFamiTF300519.

Enzyme and pathway databases

ReactomeiR-MMU-6814848. Glycerophospholipid catabolism.

Miscellaneous databases

PROiA2AJ88.
SOURCEiSearch...

Gene expression databases

BgeeiA2AJ88.
CleanExiMM_PNPLA7.
ExpressionAtlasiA2AJ88. baseline and differential.
GenevisibleiA2AJ88. MM.

Family and domain databases

Gene3Di2.60.120.10. 3 hits.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR002641. Patatin/PLipase_A2-rel.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 3 hits.
PF01734. Patatin. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 3 hits.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 3 hits.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 801-1352 (ISOFORM 2).
    Strain: 129 and FVB/N.
    Tissue: Limb and Mammary tumor.
  4. "Identification of two novel splicing variants of murine NTE-related esterase."
    Chang P.A., Wang Z.X., Long D.X., Qin W.Z., Wei C.Y., Wu Y.J.
    Gene 497:164-171(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-1352 (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    Strain: Kunming.
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiPLPL7_MOUSE
AccessioniPrimary (citable) accession number: A2AJ88
Secondary accession number(s): A9YTK0
, B0LS74, B0ZTC6, B9EJ75, Q3TD21, Q3UFP1, Q66JS2, Q6P3F9, Q8BTY7, Q8R064, Q8R3C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: February 20, 2007
Last modified: June 8, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-27 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.