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Protein

Porimin

Gene

Tmem123

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Implicated in oncotic cell death, characterized by cell swelling, organelle swelling, vacuolization and increased membrane permeability.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Porimin
Alternative name(s):
Transmembrane protein 123
Gene namesi
Name:Tmem123
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1919179. Tmem123.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 152129ExtracellularSequence analysisAdd
BLAST
Transmembranei153 – 17321HelicalSequence analysisAdd
BLAST
Topological domaini174 – 19522CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 195172PoriminPRO_0000045059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence analysis
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence analysis
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence analysis
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence analysis
Modified residuei187 – 1871PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ91Z22.
PaxDbiQ91Z22.
PRIDEiQ91Z22.

PTM databases

iPTMnetiQ91Z22.
PhosphoSiteiQ91Z22.

Expressioni

Gene expression databases

BgeeiQ91Z22.
CleanExiMM_TMEM123.
ExpressionAtlasiQ91Z22. baseline and differential.
GenevisibleiQ91Z22. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051966.

Structurei

3D structure databases

ProteinModelPortaliQ91Z22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 14498Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the CD164 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J1SC. Eukaryota.
ENOG410ZE8W. LUCA.
GeneTreeiENSGT00450000040378.
HOGENOMiHOG000115612.
HOVERGENiHBG059722.
InParanoidiQ91Z22.
OMAiYRSIDEH.
OrthoDBiEOG7SBNRV.
PhylomeDBiQ91Z22.
TreeFamiTF350123.

Family and domain databases

InterProiIPR007947. CD164_MGC24.
[Graphical view]
PANTHERiPTHR11337. PTHR11337. 1 hit.
PfamiPF05283. MGC-24. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q91Z22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALCARAALL LGVLQVLALL GAAQDPTDAQ GSASGNHSVL TSNINITENT
60 70 80 90 100
NQTMSVVSNQ TSEMQSTAKP SVLPKTTTLI TVKPATIVKI STPGVLPHVT
110 120 130 140 150
PTASKSTPNA SASPNSTHTS ASMTTPAHSS LLTTVTVSAT THPTKGKGSK
160 170 180 190
FDAGSFVGGI VLTLGVLSIL YIGCKMYYSR RGIRYRSIDE HDAII
Length:195
Mass (Da):20,178
Last modified:December 1, 2001 - v1
Checksum:i64024F8550ABC248
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251D → E in BAE42962 (PubMed:16141072).Curated
Sequence conflicti25 – 251D → E in BAE43065 (PubMed:16141072).Curated
Sequence conflicti25 – 251D → E in BAE43135 (PubMed:16141072).Curated
Sequence conflicti68 – 681A → V in BAE38780 (PubMed:16141072).Curated
Sequence conflicti106 – 1061S → T in BAE33427 (PubMed:16141072).Curated
Sequence conflicti132 – 1321L → W in BAC25282 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010163 mRNA. Translation: BAC25282.1.
AK150361 mRNA. Translation: BAE29496.1.
AK151044 mRNA. Translation: BAE30061.1.
AK152180 mRNA. Translation: BAE31011.1.
AK152423 mRNA. Translation: BAE31207.1.
AK153122 mRNA. Translation: BAE31737.1.
AK153539 mRNA. Translation: BAE32076.1.
AK155767 mRNA. Translation: BAE33427.1.
AK162610 mRNA. Translation: BAE36988.1.
AK166444 mRNA. Translation: BAE38780.1.
AK170823 mRNA. Translation: BAE42054.1.
AK172352 mRNA. Translation: BAE42962.1.
AK172553 mRNA. Translation: BAE43065.1.
AK172701 mRNA. Translation: BAE43135.1.
BC010292 mRNA. Translation: AAH10292.1.
BC086319 mRNA. Translation: AAH86319.1.
CCDSiCCDS22810.1.
RefSeqiNP_598500.1. NM_133739.2.
UniGeneiMm.283293.

Genome annotation databases

EnsembliENSMUST00000052865; ENSMUSP00000051966; ENSMUSG00000050912.
GeneIDi71929.
KEGGimmu:71929.
UCSCiuc009ocx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010163 mRNA. Translation: BAC25282.1.
AK150361 mRNA. Translation: BAE29496.1.
AK151044 mRNA. Translation: BAE30061.1.
AK152180 mRNA. Translation: BAE31011.1.
AK152423 mRNA. Translation: BAE31207.1.
AK153122 mRNA. Translation: BAE31737.1.
AK153539 mRNA. Translation: BAE32076.1.
AK155767 mRNA. Translation: BAE33427.1.
AK162610 mRNA. Translation: BAE36988.1.
AK166444 mRNA. Translation: BAE38780.1.
AK170823 mRNA. Translation: BAE42054.1.
AK172352 mRNA. Translation: BAE42962.1.
AK172553 mRNA. Translation: BAE43065.1.
AK172701 mRNA. Translation: BAE43135.1.
BC010292 mRNA. Translation: AAH10292.1.
BC086319 mRNA. Translation: AAH86319.1.
CCDSiCCDS22810.1.
RefSeqiNP_598500.1. NM_133739.2.
UniGeneiMm.283293.

3D structure databases

ProteinModelPortaliQ91Z22.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051966.

PTM databases

iPTMnetiQ91Z22.
PhosphoSiteiQ91Z22.

Proteomic databases

MaxQBiQ91Z22.
PaxDbiQ91Z22.
PRIDEiQ91Z22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052865; ENSMUSP00000051966; ENSMUSG00000050912.
GeneIDi71929.
KEGGimmu:71929.
UCSCiuc009ocx.2. mouse.

Organism-specific databases

CTDi114908.
MGIiMGI:1919179. Tmem123.

Phylogenomic databases

eggNOGiENOG410J1SC. Eukaryota.
ENOG410ZE8W. LUCA.
GeneTreeiENSGT00450000040378.
HOGENOMiHOG000115612.
HOVERGENiHBG059722.
InParanoidiQ91Z22.
OMAiYRSIDEH.
OrthoDBiEOG7SBNRV.
PhylomeDBiQ91Z22.
TreeFamiTF350123.

Miscellaneous databases

NextBioi334982.
PROiQ91Z22.
SOURCEiSearch...

Gene expression databases

BgeeiQ91Z22.
CleanExiMM_TMEM123.
ExpressionAtlasiQ91Z22. baseline and differential.
GenevisibleiQ91Z22. MM.

Family and domain databases

InterProiIPR007947. CD164_MGC24.
[Graphical view]
PANTHERiPTHR11337. PTHR11337. 1 hit.
PfamiPF05283. MGC-24. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Cerebellum, Mammary gland, Spleen and Tongue.
  2. "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].
    Strain: FVB/N-3 and NMRI.
    Tissue: Mammary tumor.
  3. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Lung.

Entry informationi

Entry nameiPORIM_MOUSE
AccessioniPrimary (citable) accession number: Q91Z22
Secondary accession number(s): Q3T9F6
, Q3TLL2, Q3U1R6, Q8CEX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 1, 2001
Last modified: January 20, 2016
This is version 94 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

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.