MIG38_CAEEL
ID MIG38_CAEEL Reviewed; 1607 AA.
AC A6ZJ71;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Abnormal cell migration protein 38 {ECO:0000312|WormBase:F40F11.2};
GN Name=mig-38 {ECO:0000312|WormBase:F40F11.2};
GN ORFNames=F40F11.2 {ECO:0000312|WormBase:F40F11.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22732572; DOI=10.1016/j.ydbio.2012.06.011;
RA Martynovsky M., Wong M.C., Byrd D.T., Kimble J., Schwarzbauer J.E.;
RT "mig-38, a novel gene that regulates distal tip cell turning during
RT gonadogenesis in C. elegans hermaphrodites.";
RL Dev. Biol. 368:404-414(2012).
CC -!- FUNCTION: During gonad development, involved in distal tip cell (DTC)
CC migration from the dorsal side of the hermaphrodite body to the midbody
CC which allows for the formation of gonad arms. Role in gonad DTC
CC migration may be in association with integrin related proteins ina-1
CC and mig-15. {ECO:0000269|PubMed:22732572}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22732572}. Cytoplasm
CC {ECO:0000269|PubMed:22732572}.
CC -!- TISSUE SPECIFICITY: Expressed in gonad distal tip cells and gonad
CC sheath cells. {ECO:0000269|PubMed:22732572}.
CC -!- DEVELOPMENTAL STAGE: Expressed in somatic gonad precursors Z1 and Z4 in
CC the gonad primordium and later in distal tip cells during the larval
CC stages. {ECO:0000269|PubMed:22732572}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. RNAi-mediated knockdown results
CC in gonad distal tip cell (DTC) migration defects whereby DTCs do not
CC migrate to the midbody of the hermaphrodite and as a consequence this
CC leads to abnormal gonadal arm formation during gonad morphogenesis.
CC RNAi-mediated knockdown specifically in gonad DTCs also result in a DTC
CC migration defect in which DTCs migrate away from the hermaphrodite
CC midbody on the dorsal basement membrane. RNAi-mediated knockdown in a
CC unc-6 mutant background results in failed gonad DTC migration to the
CC midbody of the hermaphrodite. RNAi-mediated knockdown with ina-1, mig-
CC 15 or talin in an rrf-3 mutant background results in enhanced gonad DTC
CC migration. {ECO:0000269|PubMed:22732572}.
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DR EMBL; BX284604; CAO78745.1; -; Genomic_DNA.
DR RefSeq; NP_001255569.1; NM_001268640.1.
DR AlphaFoldDB; A6ZJ71; -.
DR IntAct; A6ZJ71; 1.
DR STRING; 6239.F40F11.2; -.
DR iPTMnet; A6ZJ71; -.
DR EPD; A6ZJ71; -.
DR PaxDb; A6ZJ71; -.
DR PeptideAtlas; A6ZJ71; -.
DR PRIDE; A6ZJ71; -.
DR EnsemblMetazoa; F40F11.2.1; F40F11.2.1; WBGene00009587.
DR GeneID; 178082; -.
DR KEGG; cel:CELE_F40F11.2; -.
DR UCSC; F40F11.2b; c. elegans.
DR CTD; 178082; -.
DR WormBase; F40F11.2; CE28557; WBGene00009587; mig-38.
DR eggNOG; ENOG502QU2K; Eukaryota.
DR HOGENOM; CLU_244034_0_0_1; -.
DR InParanoid; A6ZJ71; -.
DR OMA; TQHTDRT; -.
DR OrthoDB; 526880at2759; -.
DR PRO; PR:A6ZJ71; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00009587; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015671; GSCR1_dom.
DR Pfam; PF15249; GLTSCR1; 1.
DR SUPFAM; SSF54416; SSF54416; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Nucleus; Reference proteome.
FT CHAIN 1..1607
FT /note="Abnormal cell migration protein 38"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437886"
FT REGION 14..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1607 AA; 179686 MW; 114A82EEB5D95D32 CRC64;
MSYEEDDWFS YRTEFNKRAD SPRAAGNYDF ESGNIDNIPL NDDGPLSPSQ DFDLAGTLEE
YESYDLRLSP NGGLNREDQQ PGPSGNNDGQ YHVMQNNDSF AQHMQSSNTI EYNSFEMPTV
INSNHDVGPY QDLGIDDPNS FYANQQPSTS QGNDMIINEN YEMMGPSTSY MPQIDHMNPS
GNSSSQINHQ QGMIVPQVQQ QPAKPKTTKK RPPPKKKTAA QAPDTVGTVL TKVNKLTQQI
DNNNDNQEQK IETRISAEDL VRVSALLSRL DVYQKEQAQG NNTHDQDIEA LQAEIAQVFT
KNMAMSANDA PGNSILSQIQ NLTSIGSSAS SSAQPSQPAK KAAPKRKTVP NTAKNLAQNQ
QIMPPQAQIT PTKLVMDPPT TTMVPSSSQS NHMYSNDGFT TYNQMDEPGT SQQQQYNDYR
QPPSQESMQY GHQQIIQARV VPSMNQKTHN YRQAVVFASP NTNGPSSQLQ RPQSGMDQMQ
DQQYHAQDLQ GSQVQQTFVS VQHDGQIYQE VEPTLRDFVR QGRYQGPQDA PHLRQQLITN
VNATTNKQMV HRSQDPTPSP GNLQQFGEPL QRHGSYPHSH DMRPNSHSQS QHSYSNHYDG
ATEFFDVSMQ HQDSQMSQIQ PGSQHYVQQQ ELYHPIGDQQ QMVEPESEYP VPQVTNELSE
EELRAIMEEK RQIRQKRLKD IMIDQLNRLE EPVDVTPFRN KMDVLERLLP YHHFANEEEP
VSDFDSTFQR VMDNAVHQAN SIGNRIRNIV LRDTMRSSTE WEENMILFLE TESERRKLED
DKKLADQDLS TFLRNSDIIQ NVRARRLDVE RTRLRVPRIP AHLKELDLQN GQLSSLYREY
EFDSYDENRP RGSPFVYEEP ESESESEPEA EPEPKKDNFA EPEPARGDIS PLIGFPQLSP
IPSPSRYRNE SESTFDWKDE DESPLLSPET EKINKAADQF RKEIFGTQED LDKSEPFPFE
QISEAARNQH LITAQPQLPR VDASSIGSLA SSSSTVDHSP QSIHPVFSPK AAIQSSSVQV
MKPPRSPSSV SCKLSTPCVE QSLPEESHYE GSPEIDEDYD MSPIRENEPA ELISLPISVN
MIKKEKEDST PKLKLRIPAA VLQNGIVASE DESDVAVEET IPAIRKPLKL RFNLKDIKLE
EPSPDRDVAS SRPKSRTEPP PTPEKLHVKI KASPAETTPT KLQLKEKSPA KTPVFKTPLQ
TPIKMTPSPS ESRKRRSAKI EDSPAQKKKL LNSGSSFVTP KNGLRAELDE TVERPLRIMT
DGRKIVMKIS KVSRNINHFV TPRRDKKGNL HKDLSPTNYT RLTMKLMKKK GELSVEFTET
PNKNSEEDDH KIPNIPSTST SIPPASTVVS SVSVKGRPAP ASRKSSIDTA GKDKKGQLAK
NKAAFCNRFN PFANVPSSKP STSSAVSATP STSSAVSAKL PTGKTPGRPV ALSTPRSSHK
PPQAVVAPRP NLIRTAPVVP KITVTNASES SLPSKSHIPI EVKPKLSSLL PWVSDTDESP
EQKHKLKKTM PSINLLKVKT EPPEADAVTS KPESPRASSS MSFFEDAFLR SPKRSNEPLP
VVEFSDDEEN DLAHSTFSHA TDHLLGTSNM NSSTNGSSSG LPWSTDP
