ID A0A444U1K1_ACIRT Unreviewed; 1626 AA.
AC A0A444U1K1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Nucleoporin NDC1 {ECO:0000256|ARBA:ARBA00017534};
DE AltName: Full=Transmembrane protein 48 {ECO:0000256|ARBA:ARBA00031201};
GN ORFNames=EOD39_9159 {ECO:0000313|EMBL:RXM29083.1};
OS Acipenser ruthenus (Sterlet sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7906 {ECO:0000313|EMBL:RXM29083.1, ECO:0000313|Proteomes:UP000289886};
RN [1] {ECO:0000313|EMBL:RXM29083.1, ECO:0000313|Proteomes:UP000289886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHYD16114868_AA {ECO:0000313|EMBL:RXM29083.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RXM29083.1};
RA Wei Q.;
RT "Draft Genome and Complete Hox-Cluster Characterization of the Sterlet
RT Sturgeon (Acipenser ruthenus).";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), which plays a
CC key role in de novo assembly and insertion of NPC in the nuclear
CC envelope. Required for NPC and nuclear envelope assembly, possibly by
CC forming a link between the nuclear envelope membrane and soluble
CC nucleoporins, thereby anchoring the NPC in the membrane.
CC {ECO:0000256|ARBA:ARBA00025441}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004232}. Nucleus, nuclear pore complex
CC {ECO:0000256|ARBA:ARBA00004567}.
CC -!- SIMILARITY: Belongs to the NDC1 family.
CC {ECO:0000256|ARBA:ARBA00005760}.
CC -!- SIMILARITY: Belongs to the YIP1 family.
CC {ECO:0000256|ARBA:ARBA00010596}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXM29083.1}.
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DR EMBL; SCEB01215535; RXM29083.1; -; Genomic_DNA.
DR Proteomes; UP000289886; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR019049; Nucleoporin_prot_Ndc1/Nup.
DR InterPro; IPR006977; Yip1_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13269:SF6; NUCLEOPORIN NDC1; 1.
DR PANTHER; PTHR13269; UNCHARACTERIZED; 1.
DR Pfam; PF09531; Ndc1_Nup; 2.
DR Pfam; PF04893; Yip1; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW Nuclear pore complex {ECO:0000256|ARBA:ARBA00023132};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000289886};
KW Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1262..1292
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1296..1328
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1335..1364
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 23..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1626 AA; 179197 MW; 6AC9A3588EB99616 CRC64;
MAAVDGLQFQ EFDDAENLLG ANRDATTISI GDPNEKPTNQ RRSLGNSPRE EDDDLLGNAD
SDKTELLAGQ RKSAAFWTFE YYQKFFDVDT YQVLDRIKGS VLPLPGKNFV RLYIRSNPDL
YGPFWICATL VFAIAISGNI SNFLVHLGQP QYHYMPEFRK VTIAATAIYS YAWLVPLALW
GFLMWRNSKV MNIVSYSFLE IVCVYGYSLF IYIPAAILWI IPIEWVRWIT ILVAMCLSGS
VLVITFWPAV RDDNRRIAIA TISAIIILHA LLAVGCKVVF WRAAASIAWS VLLLPASTAI
FVLLSRFSVL HPIEWITGSL NFLCGSYVIF SIILLCLVVL IIGFFILEFY TVVPSIPCTQ
IALIGKVLHP QQFIHSLVHA VMGMLVSWCA AVMIGGRYQF LTTPCIAEES AVASSMCLNE
YHLFFLLAGA FMGYSYSLLY VVGNMNYVSF PSIQQYKYLR FKGSLPLVIK HSAVQALYSV
RNYCITYFFL GVLFSSAILI FRGCTPVPSQ SLKQQATPHF KGGHPHNWSA LSGECLTILN
DLTQKLIAYQ EAVSSNGRIK PQPVGSDKRP SSSGSSATSL IEEPTSWQTP KVSMGPKTPG
SVFLRSSVAS PFTPDLGSPF GSPAMKRLTG TLDPSSPWHG SVQSPHVMRR GPKLWTSSLG
AESPLNGSPQ SGPVPVPSPV AGAQKPSIVS LWIQNRQEQV KNVLAKRVLI MYLFNKLPEA
SSQALFAESQ AHIWALEGLS HLVAASYTED RFGVVQTTLP DILGTMLTLQ EAVDKHFKLP
HASSKPARTL SSLVDTSYKT LRFALRASLK TAIYRITTTF GEHLKYSARL DSLEEKKMHS
RKTEIQMQKS TTFFGMVNNH QVPAAADLSR MTFSTYSSKS PSSAKRTGGD NQYECSLVCF
YPPYRSSGFQ DTLVPTSTTN TSSRTGLNGG GHLHPHIKQE SPSSYKALSG VPVSQEVSSG
GGGTEMRGGT ASLLHPEIEL ANNSFTNSLS SYSFNNEPGS SQGLLSAGSS RHSARLLHSG
NLKRRCISVA PAAAPSEGID ITAIICSSQM SLVATCVNGL RTNSPGISSH PRAAAGHLSG
SCKPQSPPHP CSQTEESCSL PSPGACLVSF SSSSSIGSQE PERSDCDQQL QMHLNHQQQQ
QQHTPQQQQL EQPDGLGFLM NNMAHHGVLE GCQKASFLKQ EPLDEFTQSE ELFHHHHHHH
HLHHHHRHHH SLPPPYHLHQ YINQSQNAVF HLQGQPPAAE SKPLSQPERE DSTLSGGSPD
KQVCRWIDCS AAYEQQDELV RHIEKMHIDQ RKGEDFTCFW AGCVRRYKPF NARYKLLIHM
RVHSGEKPNK CMKPYACQIP GCTKRYTDPS SLRKHVKAHS AKDQQVRKKL RPCNNLDQDL
LNECLAVQNL QTATSAQHLL NGKGGRSSGL SHEMFTGMYA GSSAHHNGQT SGLLPPTQDL
SSRHQSLEGN INSPHNHLSP LSAVENTREG ISTPLLLPPG ISPMKSVAPP AAQMEKHSSS
SSQGLAHSEQ QLAAHQKPYL HFQDQHTHEG YQGSFQSCFH YGDNYRIEQS VNDVSLAGDS
HCFNPHRQNG YPMNSAHSGS TGFGMVQEMQ SGSGQEFSPT SEENVFFQVG TFDRCLNQIS
SVYTGT
//
