MILK2_RAT
ID MILK2_RAT Reviewed; 1014 AA.
AC D3ZEN0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=MICAL-like protein 2;
DE AltName: Full=Junctional Rab13-binding protein;
DE AltName: Full=Molecule interacting with CasL-like 2;
DE Short=MICAL-L2;
GN Name=Micall2; Synonyms=Jrab;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION IN NEURITE OUTGROWTH, AND SUBCELLULAR LOCATION.
RX PubMed=20008558; DOI=10.1128/mcb.01067-09;
RA Sakane A., Honda K., Sasaki T.;
RT "Rab13 regulates neurite outgrowth in PC12 cells through its effector
RT protein, JRAB/MICAL-L2.";
RL Mol. Cell. Biol. 30:1077-1087(2010).
CC -!- FUNCTION: Effector of small Rab GTPases which is involved in junctional
CC complexes assembly through the regulation of cell adhesion molecules
CC transport to the plasma membrane and actin cytoskeleton reorganization.
CC Regulates the endocytic recycling of occludins, claudins and E-cadherin
CC to the plasma membrane and may thereby regulate the establishment of
CC tight junctions and adherens junctions. In parallel, may regulate actin
CC cytoskeleton reorganization directly through interaction with F-actin
CC or indirectly through actinins and filamins. Most probably involved in
CC the processes of epithelial cell differentiation, cell spreading and
CC neurite outgrowth. {ECO:0000269|PubMed:20008558}.
CC -!- SUBUNIT: Interacts with RAB13 (GTP-bound form); competes with RAB8A and
CC is involved in tight junctions assembly. Interacts with RAB8A; competes
CC with RAB13 and is involved in E-cadherin endocytic recycling. Interacts
CC with RAB8B. Interacts (preferentially in opened conformation) with
CC ACTN1 and ACTN4; stimulated by RAB13 activation. Interacts (via
CC calponin-homology (CH) domain) with the filamins FLNA, FLNB and FLNC
CC (via actin-binding domain) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC Recycling endosome {ECO:0000250}. Cell projection
CC {ECO:0000269|PubMed:20008558}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Cytoplasm, cytosol {ECO:0000250}.
CC -!- DOMAIN: Probably exists in a closed and an open conformation due to
CC interaction of the C-terminal coiled-coil domain with an N-terminal
CC region including the calponin-homology (CH) and the LIM zinc-binding
CC domain. The conformational change is regulated by RAB13 (By
CC similarity). {ECO:0000250}.
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DR EMBL; AABR06070698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3ZEN0; -.
DR SMR; D3ZEN0; -.
DR STRING; 10116.ENSRNOP00000031199; -.
DR iPTMnet; D3ZEN0; -.
DR PhosphoSitePlus; D3ZEN0; -.
DR PaxDb; D3ZEN0; -.
DR PeptideAtlas; D3ZEN0; -.
DR PRIDE; D3ZEN0; -.
DR UCSC; RGD:1307875; rat.
DR RGD; 1307875; Micall2.
DR VEuPathDB; HostDB:ENSRNOG00000022533; -.
DR eggNOG; ENOG502QVVF; Eukaryota.
DR InParanoid; D3ZEN0; -.
DR OMA; SELMYKM; -.
DR TreeFam; TF328311; -.
DR PRO; PR:D3ZEN0; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000022533; Expressed in duodenum and 19 other tissues.
DR ExpressionAtlas; D3ZEN0; baseline and differential.
DR Genevisible; D3ZEN0; RN.
DR GO; GO:0032432; C:actin filament bundle; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0042805; F:actinin binding; ISO:RGD.
DR GO; GO:0031005; F:filamin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028563; MICAL-L.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF53; PTHR23167:SF53; 2.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endosome; LIM domain; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Tight junction; Zinc.
FT CHAIN 1..1014
FT /note="MICAL-like protein 2"
FT /id="PRO_0000424228"
FT DOMAIN 1..107
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 187..249
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 838..985
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 1..261
FT /note="Forms an intramolecular interaction with the C-
FT terminal coiled coil domain keeping the protein in a closed
FT conformation"
FT /evidence="ECO:0000250"
FT REGION 114..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..810
FT /note="Mediates targeting to the cell plasma membrane"
FT /evidence="ECO:0000250"
FT REGION 262..394
FT /note="Necessary and sufficient for interaction with
FT actinins"
FT /evidence="ECO:0000250"
FT REGION 311..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..918
FT /note="Forms an intramolecular interaction with the N-
FT terminal Calponin-homology and LIM zinc-binding domains-
FT containing region keeping the protein in a closed
FT conformation"
FT /evidence="ECO:0000250"
FT REGION 918..1014
FT /note="Mediates interaction with RAB13 and is required for
FT transition from the closed to the open conformation"
FT /evidence="ECO:0000250"
FT COILED 845..885
FT /evidence="ECO:0000255"
FT COMPBIAS 141..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 759
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TN34"
SQ SEQUENCE 1014 AA; 108382 MW; 074B0CF3D6694CF2 CRC64;
MAAIKALQEW CRQQCEGYRD VSITNMTTSF RDGLAFCAIL HRHRPDLINF NALRKENIYE
NNKLAFQVAE EQLGIPALLD AEDMVALKIP DRLSILTYVS QYYNYFHGRS PIGGMAGMKR
PSSDSTEELS GKKKVPSQPA KLSSPVPTQR LPLSPARTNP VVQRNEGVSE RPSPKAAPGT
VGSSVSSICG VCGKHVHLVQ RHLADGRLYH RSCFRCKQCS STLHSGAYRA TGEPGVFVCT
HHSSEAVSVS PKLSNLASRQ PGGGIADTRP IGVSQKVLET NGEATPLRAR TAAWEHAGGN
RAAKGFVQTE LTPPATSRVH VGSPAGPRLP MSTVTTTSAN SKATTHVTNS SPVGWSSSAQ
SSTGTSGSRP VVSPSALGAH LSVPQGQAAS KGVKTQLNSS TDSSSTAPTP AWTSSSSRTQ
QAREKFFHNL SPAPAPAPAS SSSSHASRVP TVVTAPSGKV SPLVNTSTSK VPSATVVTVP
TSKASTVVTA PTSKAPTVVT VPISKAPTVV TAPTSKVSTV VTVPTSKAST VVTAPTSKAS
TVVTVPTGRG HVVVNTSASK VSGVVDNPAQ ESSREQALSV LRKALPGLTR AGSQAPSRSS
PATSSVLITL PKNEVPPKVP SAKLSHSTTQ AFSPTPKMEP TAPLSVGSTS WTSVSLQAGK
KSPGISPGIG KTSAVSRPQA EVKGTSGPGP TSQEGQEEGP EGWRARLKPV DKSIPSARAL
EQKEPVLAEP RAGDTPRKAS SSSDSSIHIT LTPIQQKRTP CLADSGSSLA APSPPSRRKK
LVVPPTLDVS ADWLQPELKK QDDQTRSCKE KTATWGTRES SAILDNDLVS PDEAVTSPVR
LHPNYISQEE LQRQLQDIER QLDALELRGV ELEKRLRAAE GDASEDGLMV DWFRLIHEKQ
LLLRRESELM YKSKDQCLEE RQLDLQGELR RLMEKPEGLK SPQDRKREQE LLNQYVNTVN
DRSDIVDNLD EDRLREQEED QMLESMIQNL GLQRKKSKSF LSKIWSSKSK SGQT
