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Q16849 (PTPRN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase-like N

Short name=R-PTP-N
Alternative name(s):
Islet cell antigen 512
Short name=ICA 512
Islet cell autoantigen 3
PTP IA-2
Gene names
Name:PTPRN
Synonyms:ICA3, ICA512
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length979 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Implicated in neuroendocrine secretory processes. May be involved in processes specific for neurosecretory granules, such as their biogenesis, trafficking or regulated exocytosis or may have a general role in neuroendocrine functions. Seems to lack intrinsic enzyme activity. May play a role in the regulation of secretory granules via its interaction with SNTB2. Ref.6 Ref.7

Subunit structure

Interacts with phosphorylated SNTB2, protecting it from protein cleavage by CAPN1. Dephosphorylation of SNTB2 upon insulin stimulation disrupts the interaction and results in its cleavage. Ref.8

Subcellular location

Membrane; Single-pass type I membrane protein. Note: Neuroendocrine secretory granules.

Tissue specificity

Expression is restricted to neuroendocrine cells. Found in pancreas, brain and pituitary. Ref.1

Post-translational modification

O-glycosylated with core 1 or possibly core 8 glycans. Ref.9 Ref.10

Appears to undergo multiple proteolytic cleavage at consecutive basic residues.

Miscellaneous

Autoantigen in insulin-dependent diabetes mellitus (IDDM).

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 8 subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16849-1)

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.
Isoform 2 (identifier: Q16849-2)

The sequence of this isoform differs from the canonical sequence as follows:
     479-508: KPLSLAAGVKLLEILAEHVHMSSGSFINIS → N
Note: No experimental confirmation available.
Isoform 3 (identifier: Q16849-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 By similarity
Chain35 – 979945Receptor-type tyrosine-protein phosphatase-like N
PRO_0000025451

Regions

Topological domain35 – 575541Extracellular Potential
Transmembrane576 – 60025Helical; Potential
Topological domain601 – 979379Cytoplasmic Potential
Domain709 – 969261Tyrosine-protein phosphatase
Region909 – 9157Substrate binding By similarity

Sites

Active site9091Phosphocysteine intermediate By similarity
Site448 – 4492Cleavage Potential

Amino acid modifications

Glycosylation4411O-linked (GalNAc...) Ref.9 Ref.10
Glycosylation5061N-linked (GlcNAc...) Potential
Glycosylation5241N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 9090Missing in isoform 3.
VSP_045867
Alternative sequence479 – 50830KPLSL…FINIS → N in isoform 2.
VSP_043654
Natural variant4191S → R.
Corresponds to variant rs35314717 [ dbSNP | Ensembl ].
VAR_051762

Experimental info

Sequence conflict6731S → G in BAG59024. Ref.2

Secondary structure

............................................................ 979
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A852B9063D29399D

FASTA979105,848
        10         20         30         40         50         60 
MRRPRRPGGL GGSGGLRLLL CLLLLSSRPG GCSAVSAHGC LFDRRLCSHL EVCIQDGLFG 

        70         80         90        100        110        120 
QCQVGVGQAR PLLQVTSPVL QRLQGVLRQL MSQGLSWHDD LTQYVISQEM ERIPRLRPPE 

       130        140        150        160        170        180 
PRPRDRSGLA PKRPGPAGEL LLQDIPTGSA PAAQHRLPQP PVGKGGAGAS SSLSPLQAEL 

       190        200        210        220        230        240 
LPPLLEHLLL PPQPPHPSLS YEPALLQPYL FHQFGSRDGS RVSEGSPGMV SVGPLPKAEA 

       250        260        270        280        290        300 
PALFSRTASK GIFGDHPGHS YGDLPGPSPA QLFQDSGLLY LAQELPAPSR ARVPRLPEQG 

       310        320        330        340        350        360 
SSSRAEDSPE GYEKEGLGDR GEKPASPAVQ PDAALQRLAA VLAGYGVELR QLTPEQLSTL 

       370        380        390        400        410        420 
LTLLQLLPKG AGRNPGGVVN VGADIKKTME GPVEGRDTAE LPARTSPMPG HPTASPTSSE 

       430        440        450        460        470        480 
VQQVPSPVSS EPPKAARPPV TPVLLEKKSP LGQSQPTVAG QPSARPAAEE YGYIVTDQKP 

       490        500        510        520        530        540 
LSLAAGVKLL EILAEHVHMS SGSFINISVV GPALTFRIRH NEQNLSLADV TQQAGLVKSE 

       550        560        570        580        590        600 
LEAQTGLQIL QTGVGQREEA AAVLPQTAHS TSPMRSVLLT LVALAGVAGL LVALAVALCV 

       610        620        630        640        650        660 
RQHARQQDKE RLAALGPEGA HGDTTFEYQD LCRQHMATKS LFNRAEGPPE PSRVSSVSSQ 

       670        680        690        700        710        720 
FSDAAQASPS SHSSTPSWCE EPAQANMDIS TGHMILAYME DHLRNRDRLA KEWQALCAYQ 

       730        740        750        760        770        780 
AEPNTCATAQ GEGNIKKNRH PDFLPYDHAR IKLKVESSPS RSDYINASPI IEHDPRMPAY 

       790        800        810        820        830        840 
IATQGPLSHT IADFWQMVWE SGCTVIVMLT PLVEDGVKQC DRYWPDEGAS LYHVYEVNLV 

       850        860        870        880        890        900 
SEHIWCEDFL VRSFYLKNVQ TQETRTLTQF HFLSWPAEGT PASTRPLLDF RRKVNKCYRG 

       910        920        930        940        950        960 
RSCPIIVHCS DGAGRTGTYI LIDMVLNRMA KGVKEIDIAA TLEHVRDQRP GLVRSKDQFE 

       970 
FALTAVAEEV NAILKALPQ 

« Hide

Isoform 2 [UniParc].

Checksum: AA63FE699D560D7C
Show »

FASTA950102,817
Isoform 3 [UniParc].

Checksum: BEEAF1F58AF81284
Show »

FASTA88996,261

References

« Hide 'large scale' references
[1]"Molecular cloning and identification of a receptor-type protein tyrosine phosphatase, IA-2, from human insulinoma."
Lan M.S., Lu J., Goto Y., Notkins A.L.
DNA Cell Biol. 13:505-514(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Insulinoma.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Thalamus.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 2).
Tissue: Brain.
[6]"Islet cell antigen 512 is a diabetes-specific islet autoantigen related to protein tyrosine phosphatases."
Rabin D.U., Pleasic S.M., Shapiro J.A., Yoo-Warren H., Oles J., Hicks J.M., Goldstein D.E., Rae P.M.
J. Immunol. 152:3183-3188(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 389-789, ROLE IN DIABETES MELLITUS.
Tissue: Pancreatic islet.
[7]"ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules."
Solimena M., Dirkx R. Jr., Hermel J.-M., Pleasic-Williams S., Shapiro J.A., Caron L., Rabin D.U.
EMBO J. 15:2102-2114(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, ROLE IN DIABETES MELLITUS.
[8]"Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated cleavage of ICA512 upon stimulation of insulin secretion."
Ort T., Voronov S., Guo J., Zawalich K., Froehner S.C., Zawalich W., Solimena M.
EMBO J. 20:4013-4023(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNTB2, PROTEOLYTIC PROCESSING, DEPHOSPHORYLATION.
[9]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-441, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-441, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2."
Primo M.E., Klinke S., Sica M.P., Goldbaum F.A., Jakoncic J., Poskus E., Ermacora M.R.
J. Biol. Chem. 283:4674-4681(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 468-558.
[12]"Structural genomics of protein phosphatases."
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. expand/collapse author list , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.
J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 681-979.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18983 mRNA. Translation: AAA90974.1.
AK296335 mRNA. Translation: BAG59024.1.
AC114803 Genomic DNA. Translation: AAY24038.1.
CH471063 Genomic DNA. Translation: EAW70724.1.
CH471063 Genomic DNA. Translation: EAW70726.1.
BC070053 mRNA. Translation: AAH70053.1.
X62899 mRNA. Translation: CAA44688.2.
PIRI37577.
RefSeqNP_001186692.1. NM_001199763.1.
NP_001186693.1. NM_001199764.1.
NP_002837.1. NM_002846.3.
UniGeneHs.89655.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I1YX-ray2.23A/B681-979[»]
2QT7X-ray1.30A/B468-558[»]
3N01X-ray1.30A/B470-558[»]
3N4WX-ray1.45A/B470-558[»]
3NG8X-ray1.35A/B470-558[»]
3NP5X-ray1.80A/B/C/D470-558[»]
ProteinModelPortalQ16849.
SMRQ16849. Positions 468-558, 687-976.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111762. 5 interactions.
IntActQ16849. 11 interactions.
MINTMINT-1350221.
STRING9606.ENSP00000295718.

PTM databases

PhosphoSiteQ16849.

Polymorphism databases

DMDM2499754.

Proteomic databases

PaxDbQ16849.
PeptideAtlasQ16849.
PRIDEQ16849.

Protocols and materials databases

DNASU5798.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295718; ENSP00000295718; ENSG00000054356. [Q16849-1]
ENST00000409251; ENSP00000386638; ENSG00000054356. [Q16849-2]
ENST00000423636; ENSP00000392598; ENSG00000054356. [Q16849-3]
GeneID5798.
KEGGhsa:5798.
UCSCuc002vkz.3. human. [Q16849-1]
uc002vla.3. human. [Q16849-2]

Organism-specific databases

CTD5798.
GeneCardsGC02M220118.
HGNCHGNC:9676. PTPRN.
HPAHPA007179.
MIM601773. gene.
neXtProtNX_Q16849.
PharmGKBPA34021.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000243992.
HOVERGENHBG053762.
InParanoidQ16849.
KOK07817.
OMAEVCIQDG.
OrthoDBEOG7K9K30.
PhylomeDBQ16849.
TreeFamTF351976.

Gene expression databases

ArrayExpressQ16849.
BgeeQ16849.
CleanExHS_PTPRN.
GenevestigatorQ16849.

Family and domain databases

InterProIPR021613. Receptor_IA-2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF11548. Receptor_IA-2. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16849.
GeneWikiPTPRN.
GenomeRNAi5798.
NextBio22580.
PMAP-CutDBQ16849.
PROQ16849.
SOURCESearch...

Entry information

Entry namePTPRN_HUMAN
AccessionPrimary (citable) accession number: Q16849
Secondary accession number(s): B4DK12 expand/collapse secondary AC list , F5GZS3, Q08319, Q53QD6, Q6NSL1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM