ID I3L5T4_PIG Unreviewed; 1948 AA.
AC I3L5T4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Zinc finger protein 638 {ECO:0000313|Ensembl:ENSSSCP00000019384.3};
GN Name=ZNF638 {ECO:0000313|Ensembl:ENSSSCP00000019384.3,
GN ECO:0000313|VGNC:VGNC:95281};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000019384.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000019384.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000019384.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000019384.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR PaxDb; 9823-ENSSSCP00000019929; -.
DR PeptideAtlas; I3L5T4; -.
DR Ensembl; ENSSSCT00000027413.3; ENSSSCP00000019384.3; ENSSSCG00000022708.4.
DR VGNC; VGNC:95281; ZNF638.
DR eggNOG; ENOG502QVQ7; Eukaryota.
DR GeneTree; ENSGT00940000153322; -.
DR HOGENOM; CLU_002180_0_0_1; -.
DR TreeFam; TF333921; -.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000022708; Expressed in pituitary gland and 44 other cell types or tissues.
DR ExpressionAtlas; I3L5T4; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:InterPro.
DR CDD; cd12716; RRM1_2_NP220; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR033096; ZNF638_RRM1/2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15592; MATRIN 3/NUCLEAR PROTEIN 220-RELATED; 1.
DR PANTHER; PTHR15592:SF1; ZINC FINGER PROTEIN 638; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:I3L5T4};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 745..815
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1914..1944
FT /note="Matrin-type"
FT /evidence="ECO:0000259|PROSITE:PS50171"
FT REGION 186..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1857..1902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..612
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1948 AA; 216593 MW; D901BB754728DD9C CRC64;
PSATHFVLFL ENFAPLVNSL NLGIANPLLL GPSPLHFAQI KTQLALQQLN AVASHSSTPP
YTLLNQAFLK IAMSRPRFNP RGNFPLQRPR APNPSGMRPP GPFMRPGSMG LPRFYPAGRA
RGIPHRFAGH ESYQNMGPQR MNVQVTQHRT DPRLTKEKLD FHEAQQKKGK PHGSRWDDEP
HISASVGVKQ SSVPQVTEQS PKVQSRYTKE SASSILASFG LSNEDLEELS RYPDEQLTPE
NMPLILRDIR MRKMGRRLPN LPSQSRNKET LGSEAVSSNV IDYGHASKYG YTEDPLEVRI
YDPEIPTDEV KNEFRSQPSI SASVPTPNVI CNSMFPIEDV FRQMDFPSES SSNQSFFPVE
SGTKMSGLHI SGGQSVLEPV KPVSQSISQT VNQTMNQSLI PPSMNQQPFS SELISAVSQQ
ERIPHEPVIN SSNVHGSGGG KKSYQSEADI PIQSPFGIVK ASWLPKFSHA DAQKMKRLPT
PSMMNDYYAA SPRIFPHLCS LCNVECSHLK DWIQHQNTST HIESCRQLRQ QYPDWNPEIL
PSRRNEGNRK ENETPRRRSH SPSPRRCRRS SSSHRFRRSR SPIRSMYRPR SRSPRICHRF
ISRYRSRSRS PYRMRNPFRG SPKCYRSVSP ERTARRSVRS LDRKKALEDE LQRSGHGSES
IKLKHLEAVD KGHSPAQKLK TGSGSKPSVK SISSTKSDSN IGGHCTRYKS KNLEDDTSPE
NKQVSDKTVC LQRKLRKDQS SPYGSVLLIS ELPEDGCTEE EIRKIFQPFG KVNDVLIVPY
RKEAYLEMEF KEAITAVMKY IETTPLLIKG KSVKVCVPGK KKSQVNWIYI LCDSLLMRKS
TGSVKSVVTV AAKGNKASIK TAKSGGKKSL EVKKSGIVKN KDVSKPVIVT ENSEIKTNME
VKATENGAKE TISEAASEAT ENEPVNKETE EMCVVLISDL PNKGYSIEEV HSLVKPFGSL
KDILVLSSHK KLCFSFSMLS LKKQMQANVD TIYNRFVHLD NLPEDGLQCV LCIGLQFGRV
DHHMYMSNKN KAILQLDSPE SAQSMYSFLK QNPQNIGDHV LTCTLSPKMD SSEAEAEKDP
ELGNKSPDLK NSPVDESEVQ TATDSPSVKP SEVEEESIPN IRTETFVQQE ELCEEEPEKA
LCDSYFAIEM LEVETQGEEV KVEIPLVAST PASIDLFTEN VEESVLNQQV YTSDLEKEEA
EIINTETELS TSDSAFIEER NIKGILEDSP SEAEDFLSGI TQSVIEAVTE VDKYETVSEL
VPSTCVVALV PGISTGEEQA VSTVGISEKS NMDEKEENEL NTRETRMDLQ LGTEKAEKND
DRMVAEKLEK ILAAMKEKPV ENSVTKACPN KGVGQANKPD ETSKISVLAA SNASSNKSSI
KAGMASSTKA KATASKSENQ KSFLKSVLRD EINAEKKLSA KELGLLKPTS ARSGLSENSS
KLKSPQSGVT RGGSGRISAP QGKDSKLDYR DITKQSQETE AKPSVMRRDD SNNKTLTGQN
TKNPKSTTGR SSKSKEEHLF PFNLDEFVTV DEVIEEVNPF QVKQNPLKGK RKDALKNTPS
SELNLKKKKG KISAPRVMEG ELSFVTLDEI GEEEDAAAHL AQALVTVDEV IDDEEINMEE
MVKNSNSLLT LDELIDQDDC ISHSEPKDVT VLSVAEEQDL LKQERLVTVD EIGEVEELPL
NEAADINFAT LNAKGDEGNT GRDSIGFISS QMPEDPSTLV TVDEIQDDSS DLHLVTLDEV
TEEDEDSLAD FNNLKEELNF VTVDEVGEEE DGDNDLKVEL AQNKNDHPVD KRGDRKKRAV
DTKKTKLEAL SHVGPVNENV MEEDLKTMIE RHLAAKAPTK RVRIGKTPPS EKAVMAEAAK
GEEGFQISEV DEEPGLKDSE PERKRKKIED SSSGKSVAPD VPEDLDFLVP KAGFFCPICS
LFYSGEKAMT NHCKSTRHKQ NTEMRKEA
//
