ID A0A2Y9MGU5_DELLE Unreviewed; 1913 AA.
AC A0A2Y9MGU5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE SubName: Full=Nuclear pore membrane glycoprotein 210 isoform X1 {ECO:0000313|RefSeq:XP_022418272.1};
GN Name=NUP210 {ECO:0000313|RefSeq:XP_022418272.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022418272.1};
RN [1] {ECO:0000313|RefSeq:XP_022418272.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022418272.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000256|ARBA:ARBA00004590};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004590}.
CC -!- SIMILARITY: Belongs to the NUP210 family.
CC {ECO:0000256|ARBA:ARBA00007313}.
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DR RefSeq; XP_022418272.1; XM_022562564.2.
DR FunCoup; A0A2Y9MGU5; 1767.
DR STRING; 9749.A0A2Y9MGU5; -.
DR GeneID; 111168830; -.
DR KEGG; dle:111168830; -.
DR CTD; 23225; -.
DR InParanoid; A0A2Y9MGU5; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:TreeGrafter.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR058779; Ig_NUP210_13th.
DR InterPro; IPR057586; Ig_NUP210_16th.
DR InterPro; IPR055096; Ig_NUP210_1st.
DR InterPro; IPR055097; Ig_NUP210_2nd.
DR InterPro; IPR055098; Ig_NUP210_3rd.
DR InterPro; IPR056897; Ig_NUP210_4th.
DR InterPro; IPR056898; Ig_NUP210_6th.
DR InterPro; IPR055099; Ig_NUP210_7th.
DR InterPro; IPR056899; Ig_NUP210_9th.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR045197; NUP210-like.
DR InterPro; IPR055094; NUP210_Ig15.
DR InterPro; IPR055095; NUP210_Ig_C.
DR PANTHER; PTHR23019:SF2; NUCLEAR PORE MEMBRANE GLYCOPROTEIN 210; 1.
DR PANTHER; PTHR23019; NUCLEAR PORE MEMBRANE GLYCOPROTEIN GP210-RELATED; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF26181; Ig_NUP210_13th; 1.
DR Pfam; PF26183; Ig_NUP210_14th; 1.
DR Pfam; PF22959; Ig_NUP210_15th; 1.
DR Pfam; PF25354; Ig_NUP210_16th; 1.
DR Pfam; PF22967; Ig_NUP210_1st; 1.
DR Pfam; PF22969; Ig_NUP210_2nd; 1.
DR Pfam; PF22963; Ig_NUP210_3rd; 1.
DR Pfam; PF24991; Ig_NUP210_4th; 1.
DR Pfam; PF26182; Ig_NUP210_5th; 1.
DR Pfam; PF24935; Ig_NUP210_6th; 1.
DR Pfam; PF22962; Ig_NUP210_7th; 1.
DR Pfam; PF26184; Ig_NUP210_8th; 1.
DR Pfam; PF24902; Ig_NUP210_9th; 1.
DR Pfam; PF22957; NUP210_Ig; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1913
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016116382"
FT TRANSMEM 1811..1833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1079..1158
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT REGION 1889..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1889..1898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1913
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1913 AA; 207450 MW; 61A3F23CDBB9B5C5 CRC64;
MVARGRRLWP LLLALSGLLA LGPSAPAAKL NIPKVLLPFT RATRVNFTLE ASEGCYRWSS
TRPEVASIEP LGLDEQQCSQ KAVVQARLSQ PARLTSIIFA EDITTGQVLR CDAIVDLIHG
IQIVSTTREL YLEDSPLELK IQALDSEGNT FSTLAGLVFD WMIVKDTEAD GYSDTHNALR
ILTFLESTYI PPSYISEMEK AAKQGDTILV SGMKTGSSKL KARIQEAVYK NVRPAEVRLL
ILENILLNPA YDVYLMVGTS IRYKVQKIRQ GKITELSMPS DQYELQLQNN IWGPEGDPGR
PVAVLAQDTS LVTAVQLGQS NLVLGHRSIR MQGASRLPNS TIYVVEPGYL GFTVHPGGRW
VFETGRLYEI TVEVLDKSGN KVYLSDNIHI ETTLPAEFFE VLASSQNGSY HHVRATKRGQ
TAIEAALTSV VDQDGGVHTL RVPVWNQQEV EIHVPITLYP SILTFPWQPK TGAYQYTIKA
HGGSGNFSWS SSSSVVATVT VKGVMTTGSD TGLSVIQAHD VQNPLHFGEM KVYVIEPSGM
EFAPCPVEAS MGQSLELPLR IHGLMPGGAD EVVTLSDCSH FDLAVEMENQ GVFQPLPGRL
RPGPEHCSGV TVRAEAQGYT ALLVSYKHGH IHLSARITIA AYLPLKAVDP SSVALVTLGS
SKEMLFEEGP RPWVLEPSKF FRNVTSEDMD SVSLALFGPP AARNHQQHWI LVTCQVLGEQ
VVALTVGNRP SITNPFPALE PAVVKFVCAP PSRLTLMPVY ASPQLDLSCP LLQQSKQVVP
VSSHRNPLLD LAAYDQQGRR FDNFSSLSIQ WESTRPSLAS IELDPPLQLV SRDDGSGQKK
LHGLQAISVH QASGTTAISA TATGYQQSHL DMARVKQPHH PLMPVSASIE LLLVEDVRVS
PEEVAIYNHP GVQAELHVRE GSGYFFLNTS SADVVRVAYQ EARGIATVHP LLPGTSTIMI
HDLCLAFPAP AKADVYVSDI QELYIRVVDK VEIGKTVKAY VRVLDFHKKP FLAKYLAFMD
LKLRAASQIV TLVALDEAPD DYTAVFRVHG VAIGQTSLTA TVTDKAGQRI NSAPQQIEVF
PPFRLIPRKV TLIIGATMQI TSEGGPQPQS NILFSISNES VALVGSTGLV RGLSVGHGAV
SGVVQAVDAE SGRLVVVSQD LVEVEVLLLQ AVRIRAPITR MRTETQMPVY VTGITNNQNP
FSFGNAVPGL TFHWSVTKRD ILDVRGRHHE ASLRLPSQYN FAMNVHGRVK GRTGLRVVVK
AQDPTAGQLL GLAKELSDEI QIQVFEKLRL LNPEIEAEHV LMSPNSFVKL QTNRDGAASL
SYHVLDGPEK VPIVHVDEKG FLVSGSMIGT STVEVTAQEA FGANQTIIVA VKVSPVSYLR
ISMSPALHTQ NKEALAALPL GVTVTFTVHF HDNSGDIFHA HNSVLNFATN RDEFVQIGKG
ATNNTCVVRA VSVGLTLLRA WDAAHGGLSD FVPLPVLQAI SPELSGAVVV GDVLCLATVL
VSLEGIPGTW SSSARSILHV DPKTGVAVAR EAGSVTVYYE LAGHLKTYKE IVVSVPQRIV
ARYTRPVQTS FQEVAASKVM VTVGDRSSNL RGECSPGQVE SIAALHPESL LGCQLQFKQD
IFDFPAREVF TVEPEFDAAL GRYLCSVTML RLTDKQLKHL SLKRTALLVT PSLPGSHFSG
EQVGAEVPFS PGLYTDQAEI LLSNHYTSSE VKVFGAMEVL ENLEVKSGSP AVLAFVKEKS
LGLPSFVTYT VGISDPTAGS QGPLSTTLTF SSPTTNQAIT IPVTVAFVMD RRGPGAHGAG
LFQHILDSYQ VMFFTLFALL AATAVTIIAY HAVCTPREPS TPPALSPRAS PRHSPHCWCS
WGNKILHASW TPRITAFSQA CDPRESRGLP SSSLPHVNSD SSSSCVCSGR SPC
//