NCKP1_RAT
ID NCKP1_RAT Reviewed; 1128 AA.
AC P55161;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Nck-associated protein 1;
DE Short=NAP 1;
DE AltName: Full=Membrane-associated protein HEM-2;
DE AltName: Full=p125Nap1;
GN Name=Nckap1; Synonyms=Hem2, Nap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8605018; DOI=10.1006/bbrc.1996.0264;
RA Kitamura T., Kitamura Y., Yonezawa K., Totty N.F., Gout I., Hara K.,
RA Waterfield M.D., Sakaue M., Ogawa W., Kasuga M.;
RT "Molecular cloning of p125Nap1, a protein that associates with an SH3
RT domain of Nck.";
RL Biochem. Biophys. Res. Commun. 219:509-514(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7643388; DOI=10.1006/jmbi.1995.0414;
RA Baumgartner S., Martin D., Chiquet-Ehrismann R., Sutton J., Desai A.,
RA Huang I., Kato K., Hromas R.;
RT "The HEM proteins: a novel family of tissue-specific transmembrane proteins
RT expressed from invertebrates through mammals with an essential function in
RT oogenesis.";
RL J. Mol. Biol. 251:41-49(1995).
CC -!- FUNCTION: Part of the WAVE complex that regulates lamellipodia
CC formation. The WAVE complex regulates actin filament reorganization via
CC its interaction with the Arp2/3 complex. Actin remodeling activity is
CC regulated by RAC1 (By similarity). As component of the WAVE1 complex,
CC required for BDNF-NTRK2 endocytic trafficking and signaling from early
CC endosomes (By similarity). {ECO:0000250|UniProtKB:P28660}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or
CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC WAVE1, ABI2 and BRK1. Component of the WAVE2 complex composed of ABI1,
CC CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. CYFIP2 binds to activated
CC RAC1 which causes the complex to dissociate, releasing activated WASF1.
CC The complex can also be activated by NCK1. Associates preferentially
CC with the first SH3 domain of NCK. Interacts with NYAP1, NYAP2 and MYO16
CC (By similarity). {ECO:0000250|UniProtKB:P28660,
CC ECO:0000250|UniProtKB:Q9Y2A7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P28660};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:P28660};
CC Cytoplasmic side {ECO:0000250|UniProtKB:P28660}. Cell projection,
CC lamellipodium membrane {ECO:0000250|UniProtKB:P28660}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:P28660}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P28660}. Note=At the interface between the
CC lamellipodial actin meshwork and the membrane.
CC {ECO:0000250|UniProtKB:P28660}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in brain, heart, liver and
CC testis.
CC -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family. {ECO:0000305}.
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DR EMBL; D84346; BAA12319.1; -; mRNA.
DR EMBL; X80029; CAA56333.1; -; mRNA.
DR PIR; S57833; S57833.
DR RefSeq; NP_113806.1; NM_031618.1.
DR AlphaFoldDB; P55161; -.
DR SMR; P55161; -.
DR BioGRID; 248630; 4.
DR IntAct; P55161; 2.
DR MINT; P55161; -.
DR STRING; 10116.ENSRNOP00000059233; -.
DR iPTMnet; P55161; -.
DR PhosphoSitePlus; P55161; -.
DR jPOST; P55161; -.
DR PaxDb; P55161; -.
DR PRIDE; P55161; -.
DR GeneID; 58823; -.
DR KEGG; rno:58823; -.
DR UCSC; RGD:61939; rat.
DR CTD; 10787; -.
DR RGD; 61939; Nckap1.
DR eggNOG; KOG1917; Eukaryota.
DR InParanoid; P55161; -.
DR OrthoDB; 138196at2759; -.
DR PhylomeDB; P55161; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:P55161; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031941; C:filamentous actin; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0031209; C:SCAR complex; ISO:RGD.
DR GO; GO:0045176; P:apical protein localization; ISO:RGD.
DR GO; GO:0045175; P:basal protein localization; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0010172; P:embryonic body morphogenesis; ISO:RGD.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; ISO:RGD.
DR GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
DR GO; GO:0007492; P:endoderm development; ISO:RGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
DR GO; GO:0008078; P:mesodermal cell migration; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0030903; P:notochord development; ISO:RGD.
DR GO; GO:0048570; P:notochord morphogenesis; ISO:RGD.
DR GO; GO:0048339; P:paraxial mesoderm development; ISO:RGD.
DR GO; GO:0048340; P:paraxial mesoderm morphogenesis; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISO:RGD.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; ISO:RGD.
DR InterPro; IPR019137; Nck-associated_protein-1.
DR PANTHER; PTHR12093; PTHR12093; 1.
DR Pfam; PF09735; Nckap1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cell projection; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2A7"
FT CHAIN 2..1128
FT /note="Nck-associated protein 1"
FT /id="PRO_0000216174"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 640..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2A7"
FT CONFLICT 2..30
FT /note="SRSVLQPSQQKLAEKLTILNDRGVGMLTR -> LRGTEIVYIKFVLKFFKRN
FT S (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="L -> M (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..104
FT /note="EFK -> DLR (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="D -> A (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="E -> G (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> R (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> G (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="E -> V (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="Missing (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 513..514
FT /note="GK -> ER (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="C -> Y (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 658..659
FT /note="EK -> KS (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="E -> A (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 805..806
FT /note="IA -> MP (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="G -> A (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="S -> C (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 983..993
FT /note="KSENISPEEEY -> NQRTLVQEEDI (in Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
FT CONFLICT 1033..1052
FT /note="AKAINQIAAALFTIHKGSIE -> PKPSTKLLLLCLQFTKEALK (in
FT Ref. 2; CAA56333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1128 AA; 128865 MW; 95A888A0CB0E3114 CRC64;
MSRSVLQPSQ QKLAEKLTIL NDRGVGMLTR LYNIKKACGD PKAKPSYLID KNLESAVKFI
VRKFPAVETR NNNQQLAQLQ KEKSEILKNL ALYYFTFVDV MEFKDHVCDL LNTIDVCQVF
FDITVNFDLT KNYLDLTVTY TTLMILLSRI EERKAIIGLY NYAHEMTHGA SDREYPRLGQ
MIVDYEHPLK KMMEEFVPHS KSLSDALISL QMVYPRRNLS ADQWRNAQLL SLISAPSTML
NPAQSDTMPC EYLSLDAMEK WIIFGFILCH GMLNTEATAL NLWKLALQSS SCLSLFRDEV
FHIHKAAEDL FVNIRGYNKR INDIRECKEA AVSHAGSMHR ERRKFLRSAL KELATVLSDQ
PGLLGPKALF VFMALSFARD EIIWLLRHAD NMPKKSADDF IDKHIAELIF YMEELRAHVR
KYGPVMQRYY VQYLSGFDAV VLNELVQNLS VCPEDESIIM SSFVNTMTSL SVKQVEDGEV
FDFRGMRLDW FRLQAYTSVS KASLSLADHR ELGKMMNTII FHTKMVDSLV EMLVETSDLS
IFCFYSRAFE KMFQQCLELP SQSRYSIAFP LLCTHFMSCT HELCPEERHH IGDRSLSLCN
MFLDEMAKQA RNLITDICTE QCTLSDQLLP KHCAKTISQA VNKKSKKQTG KKGEPEREKP
GVESMRKNRL VVTNLDKLHT ALSELCFSIN YVPNMAVWEH TFTPREYLTS HLEIRFTKSI
VGMTMYNQAT QEIAKPSELL TSVREYMTVL QSIENYVQID ITRVFNNVLL QQTQHLDSHG
EPTITSLYTN WYLETLLRQV SNGHIAYFPA MKAFVNLPTE NELTFNAEEY SDISEMRSLS
ELLGPYGMKF LSESLMWHIS SQVAELKKLV VENVDVLTQM RTSFDKPDQM AALFKRLSSV
DSVLKRMTII GVILSFRSLA QEALRDVLSY HIPFLVSSIE DFKDHIPRET DMKVAMNVYE
LSSAAGLPCE IDPALVVALS SQKSENISPE EEYKIACLLM VFVAVSLPTL ASNVMSQYSP
AIEGHCNNIH CLAKAINQIA AALFTIHKGS IEDRLKEFLA LASSSLLKIG QETDKTTTRN
RESVYLLLDM IVQESPFLTM DLLESCFPYV LLRNAYHAVY KQSVTSSA
