MILK1_RAT
ID MILK1_RAT Reviewed; 855 AA.
AC D3ZQL6;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=MICAL-like protein 1;
GN Name=Micall1;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-461; SER-480 AND SER-682, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION IN NEURITE OUTGROWTH, AND INTERACTION WITH EHD1 AND RAB35.
RX PubMed=23572513; DOI=10.1242/jcs.117846;
RA Kobayashi H., Fukuda M.;
RT "Rab35 establishes the EHD1-association site by coordinating two distinct
RT effectors during neurite outgrowth.";
RL J. Cell Sci. 126:2424-2435(2013).
CC -!- FUNCTION: Probable lipid-binding protein with higher affinity for
CC phosphatidic acid, a lipid enriched in recycling endosome membranes. On
CC endosome membranes, may act as a downstream effector of Rab proteins
CC recruiting cytosolic proteins to regulate membrane tubulation. May be
CC involved in a late step of receptor-mediated endocytosis regulating for
CC instance endocytosed-EGF receptor trafficking. Alternatively, may
CC regulate slow endocytic recycling of endocytosed proteins back to the
CC plasma membrane. May indirectly play a role in neurite outgrowth.
CC {ECO:0000269|PubMed:23572513}.
CC -!- SUBUNIT: Homooligomer (Probable). Interacts (via NPF1 motif) with EHD1
CC (via EH domain); the interaction is direct and probably recruits EHD1
CC to membranes. Interacts with EHD3 (via EH domain). Interacts with RAB35
CC (GTP-bound form); the interaction is direct and probably recruits
CC MICALL1 to membranes. Interacts with ACAP2; the interaction is indirect
CC through RAB35. Interacts with RAB8A (GTP-bound form); regulates RAB8A
CC association with recycling endosomes. Interacts with RAB13 (GTP-bound
CC form). Interacts with ARF6 (GTP-bound form). Interacts with PACSIN2
CC (via the SH3 domain). Interacts with DPYSL2.
CC {ECO:0000269|PubMed:23572513, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Late endosome membrane
CC {ECO:0000250}. Note=Localization to late endosomes is actin-dependent.
CC Association to tubular recycling endosomes is regulated by RAB35 and
CC ARF6 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Probably exists in a closed and an opened conformation due to
CC interaction of the C-terminal RAB-binding domain (RBD), also described
CC as bivalent Mical/EHBP Rab binding (bMERB) domain, with the N-terminal
CC calponin-homology (CH) domain. The conformational change is regulated
CC by RAB13 and may modulate MICALL1 interactions with functional partners
CC (By similarity). {ECO:0000250}.
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DR EMBL; AABR06052007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002726994.2; XM_002726948.3.
DR RefSeq; XP_002729878.2; XM_002729832.4.
DR AlphaFoldDB; D3ZQL6; -.
DR SMR; D3ZQL6; -.
DR STRING; 10116.ENSRNOP00000034618; -.
DR iPTMnet; D3ZQL6; -.
DR PhosphoSitePlus; D3ZQL6; -.
DR PaxDb; D3ZQL6; -.
DR PeptideAtlas; D3ZQL6; -.
DR PRIDE; D3ZQL6; -.
DR Ensembl; ENSRNOT00000036357; ENSRNOP00000034618; ENSRNOG00000026212.
DR GeneID; 362958; -.
DR KEGG; rno:362958; -.
DR UCSC; RGD:1305415; rat.
DR CTD; 85377; -.
DR RGD; 1305415; Micall1.
DR eggNOG; ENOG502QWQX; Eukaryota.
DR GeneTree; ENSGT00940000156057; -.
DR HOGENOM; CLU_015382_1_0_1; -.
DR InParanoid; D3ZQL6; -.
DR OMA; GHNKSTH; -.
DR OrthoDB; 377701at2759; -.
DR PhylomeDB; D3ZQL6; -.
DR TreeFam; TF328311; -.
DR PRO; PR:D3ZQL6; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000026212; Expressed in heart and 19 other tissues.
DR Genevisible; D3ZQL6; RN.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0032458; P:slow endocytic recycling; 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:SF44; PTHR23167:SF44; 1.
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 Coiled coil; Endocytosis; Endosome; LIM domain; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..855
FT /note="MICAL-like protein 1"
FT /id="PRO_0000424557"
FT DOMAIN 2..108
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 163..226
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 663..810
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 110..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..855
FT /note="Mediates the interaction with RAB13 and
FT intramolecular interaction with the calponin-homology (CH)
FT domain"
FT /evidence="ECO:0000250"
FT REGION 692..855
FT /note="Necessary and sufficient to associate with tubular
FT recycling endosome membranes, mediate phosphatidic acid-
FT binding and membrane tubulation"
FT /evidence="ECO:0000250"
FT REGION 815..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 679..703
FT /evidence="ECO:0000255"
FT COILED 794..822
FT /evidence="ECO:0000255"
FT MOTIF 423..425
FT /note="NPF1"
FT MOTIF 625..627
FT /note="NPF2"
FT COMPBIAS 281..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGT6"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGT6"
SQ SEQUENCE 855 AA; 92644 MW; A2AF8EECFF47F51C CRC64;
MAGPRGALLA WCRRQCEGYR GVDIRDLSSS FRDGLAFCAI LHRHRPDLLD FQSLSKENVF
ENNRLAFEVA EKELGIPALL DPNDMVSMSV PDCLSIMTYV SQYYNHFTSS GQAAASPPKP
GKDPAAPSPT STSPAVQPGE EAQGDDLSPD SLSEQGKPQP PSSACAACGQ RVHLVQRYLA
EGRLYHRHCF RCRQCSSTLV PGSYSSGPEE GTFVCAERCT RLGLGGRSGT RPLSLQKQQP
AAAAEAKDGE DSDLSKSVVV VAAEADGLQA SSEVQPHTLT KPPLPSKPQD LASPPVSRPT
PAPRKASESS ALTPPTPRPR SSLQQDGMVE QSVSGDLVNG RLQELPVPKP RGTPKLSERM
TAPRKDPPWI TLVQTEPKKK PAPLPPSSGP GPLSQASRQV ENGGLEEKTQ KSPAAEPEPK
PYNPFEEEEE EEEASVPAVP SPAPAPPETT PKSLHPWYNI TPTSSPKTKK RPAPKAPSAS
PLVLHASRLS HSEPPSATPS PALSVESLSS ESSSHTANTE PSEPPAVPKS SSDPAVHVPG
TPGTSANSVT PSAHSSLSSS GELGQPSGEQ MPQARTRGSP GTHSTKPFSG ATPTPFLLAG
DQKSPAPPMG SSSPQMLIKS SCKENPFNRK PSPSTSPTVR KATKGAKPVR PPAPGHGFPL
IKRKVQADQY IPEEDIYGEM DSIERQLDAL EHSGVLLEEK LRGGANEGSE DDMLVDWFKL
IHEKHLLVRR ESELIYVFKQ QNLEQRQADV EFELRCLLNK PEKDWTDDDR AREKVLMQEL
MTLIEQRDAI VNCLDEDRQR EEEEDKMLET MIKKKDFQRE AESDSKKKGK FKTMKVLKLL
GNKRDAKSKA PTGKS
