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Protein

Single-pass membrane and coiled-coil domain-containing protein 3

Gene

SMCO3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Single-pass membrane and coiled-coil domain-containing protein 3
Gene namesi
Name:SMCO3
Synonyms:C12orf69
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:34401. SMCO3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei155 – 17521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162378005.

Polymorphism and mutation databases

BioMutaiSMCO3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Single-pass membrane and coiled-coil domain-containing protein 3PRO_0000336988Add
BLAST

Proteomic databases

EPDiA2RU48.
PaxDbiA2RU48.
PRIDEiA2RU48.

PTM databases

iPTMnetiA2RU48.

Expressioni

Gene expression databases

BgeeiA2RU48.
CleanExiHS_C12orf69.
GenevisibleiA2RU48. HS.

Organism-specific databases

HPAiHPA040574.
HPA047804.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK9P459843EBI-10173195,EBI-713568
TRIM39Q9HCM93EBI-10173195,EBI-739510

Protein-protein interaction databases

BioGridi136283. 4 interactions.
IntActiA2RU48. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliA2RU48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili62 – 9231Sequence analysisAdd
BLAST
Coiled coili183 – 20725Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPT6. Eukaryota.
ENOG411198U. LUCA.
GeneTreeiENSGT00390000013440.
HOGENOMiHOG000111771.
HOVERGENiHBG095374.
InParanoidiA2RU48.
OMAiCDIIIQA.
OrthoDBiEOG7NPFV5.
PhylomeDBiA2RU48.
TreeFamiTF335698.

Family and domain databases

InterProiIPR027895. DUF4533.
[Graphical view]
PfamiPF15047. DUF4533. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2RU48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSDFLYPE NPKRREEVNR LHQQLLDCLS DSFDVTNKLT EVLNMHLGCR
60 70 80 90 100
LASIEMKRDG TIKENCDLII QAIMKIQKEL QKVDEALKDK LEPTLYRKLQ
110 120 130 140 150
DIKEKETDKI AIVQKVISVI LGEATSAASA VAVKLVGSNV TTGIINKLVT
160 170 180 190 200
VLAQIGASLL GSIGVAVLGL GIDMIVRAIL GAVEKTQLQA AIKSYEKHLV
210 220
EFKSASEKYN HAITEVINTV KHQMK
Length:225
Mass (Da):24,877
Last modified:March 6, 2007 - v1
Checksum:i0B80F5E0FF66CD20
GO

Sequence cautioni

The sequence BAC03930.1 differs from that shown. Reason: Frameshift at position 219. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491C → R.
Corresponds to variant rs11609202 [ dbSNP | Ensembl ].
VAR_043558
Natural varianti75 – 751K → R.
Corresponds to variant rs2241221 [ dbSNP | Ensembl ].
VAR_043559

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK092637 mRNA. Translation: BAC03930.1. Frameshift.
AC007655 Genomic DNA. No translation available.
BC132752 mRNA. Translation: AAI32753.1.
BC132754 mRNA. Translation: AAI32755.1.
CH471094 Genomic DNA. Translation: EAW96331.1.
CCDSiCCDS41759.1.
RefSeqiNP_001013720.2. NM_001013698.2.
UniGeneiHs.220931.

Genome annotation databases

EnsembliENST00000316048; ENSP00000381895; ENSG00000179256.
GeneIDi440087.
KEGGihsa:440087.
UCSCiuc001rck.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK092637 mRNA. Translation: BAC03930.1. Frameshift.
AC007655 Genomic DNA. No translation available.
BC132752 mRNA. Translation: AAI32753.1.
BC132754 mRNA. Translation: AAI32755.1.
CH471094 Genomic DNA. Translation: EAW96331.1.
CCDSiCCDS41759.1.
RefSeqiNP_001013720.2. NM_001013698.2.
UniGeneiHs.220931.

3D structure databases

ProteinModelPortaliA2RU48.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi136283. 4 interactions.
IntActiA2RU48. 2 interactions.

PTM databases

iPTMnetiA2RU48.

Polymorphism and mutation databases

BioMutaiSMCO3.

Proteomic databases

EPDiA2RU48.
PaxDbiA2RU48.
PRIDEiA2RU48.

Protocols and materials databases

DNASUi440087.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316048; ENSP00000381895; ENSG00000179256.
GeneIDi440087.
KEGGihsa:440087.
UCSCiuc001rck.1. human.

Organism-specific databases

CTDi440087.
GeneCardsiSMCO3.
HGNCiHGNC:34401. SMCO3.
HPAiHPA040574.
HPA047804.
neXtProtiNX_A2RU48.
PharmGKBiPA162378005.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPT6. Eukaryota.
ENOG411198U. LUCA.
GeneTreeiENSGT00390000013440.
HOGENOMiHOG000111771.
HOVERGENiHBG095374.
InParanoidiA2RU48.
OMAiCDIIIQA.
OrthoDBiEOG7NPFV5.
PhylomeDBiA2RU48.
TreeFamiTF335698.

Miscellaneous databases

GenomeRNAii440087.
PROiA2RU48.

Gene expression databases

BgeeiA2RU48.
CleanExiHS_C12orf69.
GenevisibleiA2RU48. HS.

Family and domain databases

InterProiIPR027895. DUF4533.
[Graphical view]
PfamiPF15047. DUF4533. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
    , 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].
    Tissue: Prostate.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].

Entry informationi

Entry nameiSMCO3_HUMAN
AccessioniPrimary (citable) accession number: A2RU48
Secondary accession number(s): Q8NAI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 6, 2007
Last modified: June 8, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations

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.