ID A0A493TM83_ANAPP Unreviewed; 1370 AA.
AC A0A493TM83;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Ras and Rab interactor 2 {ECO:0000313|Ensembl:ENSAPLP00000026992.1};
GN Name=RIN2 {ECO:0000313|Ensembl:ENSAPLP00000026992.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000026992.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000026992.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000026992.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in)
CC + 4 Na(+)(out); Xref=Rhea:RHEA:69967, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00033627};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC24A subfamily. {ECO:0000256|ARBA:ARBA00005364}.
CC -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC {ECO:0000256|ARBA:ARBA00006919}.
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DR Ensembl; ENSAPLT00000025864.1; ENSAPLP00000026992.1; ENSAPLG00000014865.2.
DR GeneTree; ENSGT00940000154866; -.
DR Proteomes; UP000016666; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd16131; RA_Rin2; 1.
DR CDD; cd10394; SH2_RIN2; 1.
DR Gene3D; 1.20.1420.30; NCX, central ion-binding region; 2.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR InterPro; IPR004481; K/Na/Ca-exchanger.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR035868; RIN2_SH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR10846; SODIUM/POTASSIUM/CALCIUM EXCHANGER; 1.
DR PANTHER; PTHR10846:SF42; SODIUM_POTASSIUM_CALCIUM EXCHANGER 3; 1.
DR Pfam; PF01699; Na_Ca_ex; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF109993; VPS9 domain; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Signal {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}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1370
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019809334"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 577..670
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1097..1236
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT DOMAIN 1266..1357
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 273..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 153642 MW; 6F042909D5A26907 CRC64;
MGFDYPFHWF DTTSLILCVC DLALTALQVW PSHPSSYSTS SLRKPVHLIP AISSPCPSVH
GDSFHRVTGL TMALAVDMAV VLVRAWLTSF LCLFSQVVAL SSWSLLRDSI YYTLSVVALI
VFIYDEKVSW WESLVLVLMY AIYIVIMKYN STIHHCFERK TKNAANMVNG LANNTEMDDN
SNCDATVVLL KKGNFHRKAS VIMVDELLSA YPHQLSFSEA GLRIMITSHF PPKTRLSMAS
RMLINERQRL INSRTYTNGE SEVAIKIPIK HVVENGTGPS NSAERSMNST RREEDTAEAG
TETENENEDN ENNENDEEED EDDDNDDHEG PYTPFDLPTG KTEVLKWLFT WPLSFVLYFT
VPNCNKPHLE KWFMVTFASS TLWIAAFSYM MVWMVTIIGY TLGIPDVIMG ITFLAAGTSV
PDCMASLIVA RQGMGDMAVS NSIGSNVFDI LIGLGLPWAL QTLAVNYGSY DFKTFSGVFP
GTMSSLTMKA HCLDKRGSFF KLIDTIASEI GELKHEMVQT DLTVEDESAD LQSLVKDMGN
VSPEKKDVKG CPRDSGYDSL SNKLSILDKL LHTHPVWLQL GLNDAEAMEI LRAQPAGIFL
VRKSARLQKK VISLRLPSDC GSCLKEFAIK ESTYTFSLEG SGISFADLFR LIAFYCISRD
VLPFTLKLPH AIAAAKTEIE LEEIAQLGLN FWSSPANSNP PDPSPPRRPV PLDSACKGSR
QLCLINGVHS IRTRTPSELE CSQTNGALCF INPLFLKVHS QDVSGSLKRQ SLRSQDLNGT
ERPRSPPPRP PPPSINSILT SPQLSRTIKQ ASMPETVNHK KERDLDLLQN KPAPIPPPRL
KKQAVCVEVE GSPKTAAVIR PVCSSVPVPE AAGVPGETPP EPALAVSKKS VATSSESYTP
RNGGRQRLSD MSISTSSSDS LDFDRSMPLF GYEGDTNSSL EDFEGESDQE SMAPPLKPKK
KRNSSFVLPK IVKSQLRKVS GVFSSFMTPE KRMIKKIAEM SQDKRTYFGC LVQDYISFLQ
ENKECHVSST DMLQTIRQFM TQVKNYLSQS SELDPPIESL IPEDQIDVVL EKAMHKCILK
PLKGHIEAML KEFHTADGSW KQLKENLQLV RQRNPQELGV FVPTPDFVDV EKIKVKFMTM
QKMYSPEKKV MLLLRVCKLI YTVMENNSGR LYGADDFLPV LTYVLAQCDM LELDTEIEYM
MELLDPSLLH GEGGYYLTSA YGALSLIKNF QEEQAARLLS SEARDTLRQW HKRRTTNRTI
PSVDDFQNYL RVAFQEVNSG CTGKTLLVRP YITTEDVCQL CAEKFKVDNP KEYSLFLFVD
DTWQQLTEDT YPQKIKAELH SRPQPQVFHF VYKRINSDPY GAIFQNNSAS
//
