MILK1_BOVIN
ID MILK1_BOVIN Reviewed; 853 AA.
AC E1BBG2;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=MICAL-like protein 1;
GN Name=MICALL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP INTERACTION WITH EHD1.
RX PubMed=19864458; DOI=10.1091/mbc.e09-06-0535;
RA Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.;
RT "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor
RT recycling.";
RL Mol. Biol. Cell 20:5181-5194(2009).
RN [3]
RP INTERACTION WITH DPYSL2.
RX PubMed=20801876; DOI=10.1074/jbc.c110.166066;
RA Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.;
RT "Collapsin response mediator protein-2 (Crmp2) regulates trafficking by
RT linking endocytic regulatory proteins to dynein motors.";
RL J. Biol. Chem. 285:31918-31922(2010).
RN [4]
RP INTERACTION WITH PACSIN2.
RX PubMed=23596323; DOI=10.1091/mbc.e13-01-0026;
RA Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.;
RT "Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular
RT recycling endosome biogenesis.";
RL Mol. Biol. Cell 24:1776-1790(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 (By
CC similarity). {ECO:0000250}.
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:19864458, ECO:0000269|PubMed:20801876,
CC ECO:0000269|PubMed:23596323, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DAAA02014645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BBG2; -.
DR SMR; E1BBG2; -.
DR IntAct; E1BBG2; 1.
DR STRING; 9913.ENSBTAP00000026064; -.
DR PaxDb; E1BBG2; -.
DR PRIDE; E1BBG2; -.
DR eggNOG; ENOG502QWQX; Eukaryota.
DR HOGENOM; CLU_015382_1_0_1; -.
DR InParanoid; E1BBG2; -.
DR OrthoDB; 377701at2759; -.
DR TreeFam; TF328311; -.
DR Proteomes; UP000009136; Unplaced.
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: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; IEA:InterPro.
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; ISS:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; ISS: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..853
FT /note="MICAL-like protein 1"
FT /id="PRO_0000424556"
FT DOMAIN 2..108
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 162..224
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 661..808
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 118..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..853
FT /note="Mediates the interaction with RAB13 and RAB35 and
FT intramolecular interaction with the CH domain"
FT /evidence="ECO:0000250"
FT REGION 690..853
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 COILED 671..701
FT /evidence="ECO:0000255"
FT COILED 791..820
FT /evidence="ECO:0000255"
FT MOTIF 419..421
FT /note="NPF1"
FT MOTIF 623..625
FT /note="NPF2"
FT COMPBIAS 145..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGT6"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGT6"
SQ SEQUENCE 853 AA; 92095 MW; 8437D72B2161E7F4 CRC64;
MAGPRGALLA WCRRQCEGYR GVDIRDLSSS FRDGLAFCAI LHRHRPDLLD FDSLSKDNVF
ENNRLAFEVA EKELGIPALL DPNDMVSMSV PDCLSIMTYV SQYYNHFAGS GPAGVSSPRK
GLVLSSPPSE ASTPADPGDR AQGEECSSGS LSKQGSHRTP SSTCAACQQH VHLVQRYLAD
GKLYHRHCFR CRRCSSTLLP GAYRNGPEEG TFVCAEHCAR LGPSGRSGAR PGTPPQPKQQ
QLTEEAKEVE GGSPSPKATA GAEADVPKAS PEGRPQVPTK PRVPGRPQEL ASPPASRPTP
APRKASESTA PTPPTPRPRS SLQQENLVEQ GGGSGLVNGK LQEPPIPKPR GTPKLSERTP
APRKDPPWIT LVQAEPKKKP APLPPSSSPG PPPGQEGRQV ENGGVDKAAP RGPEPKPYNP
FEEEEEEPPA APSPAPGPAP TPPESTPKSL HPWYGITPTS SPKTKKRPAP RAPSTSPLTL
HASRLSRSEP PSATPSPALS VESLSSESSS QAPSEELLEP PVVPKSSSEP AVHAPGTPGT
SASLSANSSL SSSGELVQPS MDRTPQASPG LAPNSRGSPG PPPAKPCSGT APTPLVLVGD
KSPAPSPGTS SPQLQVKSSC KENPFNRKPS PTASPSVKKA TKGSKPARPP APGHGFPLIK
RKVQSDQYIP EEDIHGEIDT IERQLDALEH RGVLLEEKLR GGVNEGREDD MLVDWFKLIH
EKHLLVRRES ELIYVFKQQN LEQRQADVEY ELRCLLNKPE KDWTEEDRGR EKVLMQELVT
LIEQRNAIVN CLDEDRQREE EEDKMLEAMI KKKEFQKETE PEGKKKGKFK TMKVLKLLGN
KRDTKSKCPG DRS
