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Protein

Microtubule cross-linking factor 1

Gene

Mtcl1

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

Functioni

Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation. Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells.1 Publication

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  • microtubule bundle formation Source: UniProtKB
  • positive regulation of microtubule motor activity Source: UniProtKB
  • positive regulation of protein targeting to membrane Source: UniProtKB
  • regulation of autophagy Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule cross-linking factor 1
Alternative name(s):
Coiled-coil domain-containing protein 165
PAR-1-interacting protein
SOGA family member 2
Gene namesi
Name:Mtcl1
Synonyms:Ccdc165, Kiaa0802, Soga2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1915867. Mtcl1.

Subcellular locationi

Isoform 1 :
  • Lateral cell membrane
  • Apical cell membrane
  • Cytoplasmcytoskeletonspindle pole
  • Midbody
  • Cytoplasmcytoskeleton

  • Note: Colocalized with microtubules at the base of cilia. Gradually accumulates on the apicobasal microtubule bundles during epithelial cell polarization (By similarity). Colocalized with the apicobasal microtubule bundles running beneath the lateral membrane. Colocalized with microtubule bundles in the spindle pole in mitotic cells and in the midbodies at the end of cytokinesis.By similarity

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • apicolateral plasma membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB
  • extracellular space Source: InterPro
  • lateral plasma membrane Source: UniProtKB
  • microtubule bundle Source: UniProtKB
  • midbody Source: UniProtKB
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002801141 – 1945Microtubule cross-linking factor 1Add BLAST1945

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74PhosphoserineBy similarity1
Modified residuei84PhosphoserineBy similarity1
Modified residuei209PhosphoserineCombined sources1
Modified residuei213PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei541PhosphoserineBy similarity1
Modified residuei610PhosphoserineBy similarity1
Modified residuei613PhosphothreonineBy similarity1
Modified residuei677PhosphoserineBy similarity1
Modified residuei768PhosphoserineCombined sources1
Modified residuei891PhosphoserineBy similarity1
Modified residuei913PhosphoserineBy similarity1
Modified residuei1270PhosphoserineBy similarity1
Modified residuei1371PhosphoserineBy similarity1
Modified residuei1385PhosphoserineBy similarity1
Modified residuei1403PhosphothreonineCombined sources1
Modified residuei1407PhosphoserineCombined sources1
Modified residuei1413PhosphotyrosineBy similarity1
Modified residuei1501PhosphoserineBy similarity1
Modified residuei1510PhosphoserineBy similarity1
Modified residuei1577PhosphoserineBy similarity1
Modified residuei1586PhosphoserineBy similarity1
Modified residuei1655PhosphoserineBy similarity1
Modified residuei1661PhosphothreonineBy similarity1
Modified residuei1669PhosphothreonineBy similarity1
Modified residuei1673PhosphoserineBy similarity1
Modified residuei1677PhosphoserineBy similarity1
Modified residuei1778PhosphoserineBy similarity1
Modified residuei1795PhosphoserineBy similarity1
Modified residuei1799PhosphoserineCombined sources1
Modified residuei1801PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3UHU5.
PaxDbiQ3UHU5.
PeptideAtlasiQ3UHU5.
PRIDEiQ3UHU5.

PTM databases

iPTMnetiQ3UHU5.
PhosphoSitePlusiQ3UHU5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000052105.
CleanExiMM_1110012J17RIK.
ExpressionAtlasiQ3UHU5. baseline and differential.
GenevisibleiQ3UHU5. MM.

Interactioni

Subunit structurei

Homodimer. Isoform 1 interacts with MARK2; the interaction increases MARK2 microtubule-binding ability. Associates (via N- and C-terminus domains) with microtubule filaments.1 Publication

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000083899.

Structurei

3D structure databases

ProteinModelPortaliQ3UHU5.
SMRiQ3UHU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 500Necessary for self-assembly, microtubule bundling activity and apicobasal microtubule organizationAdd BLAST500
Regioni1 – 241Necessary for colocalization and binding with microtubulesAdd BLAST241
Regioni1257 – 1368Necessary for interaction with MARK2 and apicobasal microtubule bundle formation in polarized epithelial cellsBy similarityAdd BLAST112
Regioni1672 – 1767Necessary for colocalization and binding with microtubulesBy similarityAdd BLAST96

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili320 – 396Sequence analysisAdd BLAST77
Coiled coili424 – 712Sequence analysisAdd BLAST289
Coiled coili1120 – 1196Sequence analysisAdd BLAST77
Coiled coili1229 – 1270Sequence analysisAdd BLAST42

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi42 – 174Pro-richAdd BLAST133
Compositional biasi848 – 853Poly-Gly6
Compositional biasi1357 – 1360Poly-Glu4

Sequence similaritiesi

Belongs to the SOGA family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4787. Eukaryota.
ENOG410XUHJ. LUCA.
GeneTreeiENSGT00530000063889.
HOVERGENiHBG080205.
InParanoidiQ3UHU5.
OMAiEFNSKSW.
OrthoDBiEOG091G03VQ.
PhylomeDBiQ3UHU5.
TreeFamiTF331853.

Family and domain databases

InterProiIPR027882. DUF4482.
IPR027881. SOGA.
[Graphical view]
PfamiPF14818. DUF4482. 1 hit.
PF11365. SOGA. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q3UHU5-1) [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
METLNGPAGG GAPDTKPQPA GQHHRHHHLH PLAERRRLHR APSPARPFLK
60 70 80 90 100
DLHTRPATAT PSAGRAPTPA APRSPSLAGK APPSPGPPAA PGRLSRRSGV
110 120 130 140 150
VPGAKDKPPP GAGARSAGGA KAVPGTRRAA RAGPAEPLSR VGRPTGAEPP
160 170 180 190 200
PAVAKGRKTK RGPGTPPARA VVPPARASRV PAVTLSVTSV AGCRINHTDS
210 220 230 240 250
SSDLSDCASE PLSDEQRLLP AASSDAESGT GSSDREPIRG APTPSSGSRG
260 270 280 290 300
PPPGSPEPPI LLAAPPVASA CLGGRSSPGG ASTGSPGPGS QEDVGGRAPP
310 320 330 340 350
ERTILGTSKE PSLGEQPRLL VVAEEEELLR EMEELRSEND YLKDELDELR
360 370 380 390 400
AEMEEMRDSY LEEDGYQLQE LRRELDRANK NCRILQYRLR KAEQKSLKVA
410 420 430 440 450
ETGQVDGELI RSLEQDLKVA KDVSVRLHHE LETVEEKRAK AEDDNETLRQ
460 470 480 490 500
QMIEVEVSRQ ALQNEVERLR ESSLKRRGSR EMYKEKKLVN QDDSADLKCQ
510 520 530 540 550
LQFVKEEASL MRKKMAKLGR EKDELEQELQ KYKSLYGDVD SPLPTGEAGG
560 570 580 590 600
PPSTREAELK LRLKLVEEEA SILGRKIVEL EVENRGLKAE MEDIRVQHER
610 620 630 640 650
EGTGRDHVPS TPTSPFGDSM ESSTELRRHL QFVEEEAELL RRSISEIEDH
660 670 680 690 700
NRQLTHELSK FKFEPHQESG WLGDGVSKGP AASVPLQEEL KSARLQIDEL
710 720 730 740 750
SGKVLKLQCE NRLLLSNAQR GDLAAHLGLR APSPRDSDAE SDAGKKESDG
760 770 780 790 800
EEGRLPQPKR EGPVGGESDS EDMFEKTSGF GSGKPSEASE PCPAELLRVR
810 820 830 840 850
EDTECLVTIK LEAQRLERTV ERLISDTDGF IHDSGLRGNG LASPGVQGGG
860 870 880 890 900
GEGNSPSEPH LLETINVRMK AFRKELQAFL EQMSRIVDGL SPLSHLTESS
910 920 930 940 950
SFLSTVTSVS RDSPIGTLGK ELGPDLQSKL REQLEWQLNQ DRGDEREGLR
960 970 980 990 1000
LRATRELHRR ADGDSGSHHG LGGQSCFNLE MEEDHLYALR WKELEMHSLA
1010 1020 1030 1040 1050
LQNTLHKRTW SDEKNLLQQE LRSLKQNIFL FYVKLRWLLK HWRQGKQMEE
1060 1070 1080 1090 1100
GGEDLEESEH PENVPGLAEL GVQGVHQTDG IDQEDADQGC SLPMGEHAPH
1110 1120 1130 1140 1150
SLVQISEHGS RLQSSDGGPL NKQVVENQQL FRALKALLED FRSELREDEH
1160 1170 1180 1190 1200
ARLRLQQQYA SDKAAWDVEW AVLKCRLEQL EEKTEKSLGE LDSSAEGKGA
1210 1220 1230 1240 1250
LKKEREVHQK LLADSHSLVM DLRWQIHHRE KNWNREKVEL LERLDSERQE
1260 1270 1280 1290 1300
WGRQKEELLW RVEQLQKEKS PRRSGSFLCS RREDDTRPYP HQGSLHSSRP
1310 1320 1330 1340 1350
VSMWPCEDAD SIPFEDRPLS KLKESDRCSA SENLYLDALS LDDDPGDPPP
1360 1370 1380 1390 1400
LRNCLAEEEE SRKGNLQRAV SVSCMSEFQR LMDVSPFLPE KGLPSAGSKE
1410 1420 1430 1440 1450
DVTPPLSPDD LKYIEEFHSN DWDYASPRAE ADRPPDPWAD RTEMGRVGHE
1460 1470 1480 1490 1500
ATTEPCPDPS WYLTTSVTMT TDTMTSPEHC QKQPLRTHVL TEQSGVHVLH
1510 1520 1530 1540 1550
SPPAIRRVDS IASGGEGRSR ADPEGPFPMS RARGNLADAK GGHPEPVLNR
1560 1570 1580 1590 1600
WPCTPPRHPR DCVEGSLRPL DRPICPSLGF ASPLNSLDMS KNMSDDMKEV
1610 1620 1630 1640 1650
AFSVRNAICA GPAEPHVRDM ACQTNGSRTA GTQTIQTISV GLQTEALRAS
1660 1670 1680 1690 1700
GVTSSPHKCL TPKAGGGTTP VSSPSRSLRS RQVAPAIEKV QAKFERTCCS
1710 1720 1730 1740 1750
PKYGSPKLQR KPLSKADQPN SRTSPGIPQK GFSESAWARS TTTRESPVHT
1760 1770 1780 1790 1800
TINDGLSSLF NIIDHSPIGV RAGSRSRSAE PRQELGPGQE TGTSSRGRSP
1810 1820 1830 1840 1850
SPLGVGSETF REEGGESTPV RQDLSAPPGY TLTENVARIL NKKLLEHALK
1860 1870 1880 1890 1900
EERKQASHGS SGLTSDSHTG EPVPAEPGSM EELPCSALAP SLEPCFSRPE
1910 1920 1930 1940
RPANRRLPSR WAPPSPTASQ SQSPGHPMSM EEHGEEDPPE EKPHL
Length:1,945
Mass (Da):213,862
Last modified:October 11, 2005 - v1
Checksum:i7785C70146349A03
GO
Isoform 2 (identifier: Q3UHU5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-514: Missing.

Note: No experimental confirmation available.
Show »
Length:1,431
Mass (Da):158,849
Checksum:iE1CACE2324D72CBE
GO
Isoform 3 (identifier: Q3UHU5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1882-1945: ELPCSALAPS...EDPPEEKPHL → NQTVLLTAPWGL

Note: No experimental confirmation available.
Show »
Length:1,893
Mass (Da):208,107
Checksum:i35F42BAF55F50C06
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0235551 – 514Missing in isoform 2. 1 PublicationAdd BLAST514
Alternative sequenceiVSP_0235561882 – 1945ELPCS…EKPHL → NQTVLLTAPWGL in isoform 3. 1 PublicationAdd BLAST64

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147205 mRNA. Translation: BAE27762.1.
BC060225 mRNA. Translation: AAH60225.1.
AK122373 mRNA. Translation: BAC65655.1.
CCDSiCCDS28946.2. [Q3UHU5-1]
CCDS50168.1. [Q3UHU5-3]
RefSeqiNP_001107570.1. NM_001114098.1. [Q3UHU5-3]
NP_766551.3. NM_172963.4. [Q3UHU5-1]
UniGeneiMm.33421.
Mm.456506.

Genome annotation databases

EnsembliENSMUST00000086693; ENSMUSP00000083899; ENSMUSG00000052105. [Q3UHU5-1]
ENSMUST00000097291; ENSMUSP00000094894; ENSMUSG00000052105. [Q3UHU5-3]
GeneIDi68617.
KEGGimmu:68617.
UCSCiuc008djv.2. mouse. [Q3UHU5-3]
uc008djw.2. mouse. [Q3UHU5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147205 mRNA. Translation: BAE27762.1.
BC060225 mRNA. Translation: AAH60225.1.
AK122373 mRNA. Translation: BAC65655.1.
CCDSiCCDS28946.2. [Q3UHU5-1]
CCDS50168.1. [Q3UHU5-3]
RefSeqiNP_001107570.1. NM_001114098.1. [Q3UHU5-3]
NP_766551.3. NM_172963.4. [Q3UHU5-1]
UniGeneiMm.33421.
Mm.456506.

3D structure databases

ProteinModelPortaliQ3UHU5.
SMRiQ3UHU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000083899.

PTM databases

iPTMnetiQ3UHU5.
PhosphoSitePlusiQ3UHU5.

Proteomic databases

MaxQBiQ3UHU5.
PaxDbiQ3UHU5.
PeptideAtlasiQ3UHU5.
PRIDEiQ3UHU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086693; ENSMUSP00000083899; ENSMUSG00000052105. [Q3UHU5-1]
ENSMUST00000097291; ENSMUSP00000094894; ENSMUSG00000052105. [Q3UHU5-3]
GeneIDi68617.
KEGGimmu:68617.
UCSCiuc008djv.2. mouse. [Q3UHU5-3]
uc008djw.2. mouse. [Q3UHU5-1]

Organism-specific databases

CTDi23255.
MGIiMGI:1915867. Mtcl1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4787. Eukaryota.
ENOG410XUHJ. LUCA.
GeneTreeiENSGT00530000063889.
HOVERGENiHBG080205.
InParanoidiQ3UHU5.
OMAiEFNSKSW.
OrthoDBiEOG091G03VQ.
PhylomeDBiQ3UHU5.
TreeFamiTF331853.

Miscellaneous databases

PROiQ3UHU5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000052105.
CleanExiMM_1110012J17RIK.
ExpressionAtlasiQ3UHU5. baseline and differential.
GenevisibleiQ3UHU5. MM.

Family and domain databases

InterProiIPR027882. DUF4482.
IPR027881. SOGA.
[Graphical view]
PfamiPF14818. DUF4482. 1 hit.
PF11365. SOGA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTCL1_MOUSE
AccessioniPrimary (citable) accession number: Q3UHU5
Secondary accession number(s): Q6PAM2, Q80TR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 11, 2005
Last modified: November 2, 2016
This is version 83 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.