ID   KIP1_PETIN              Reviewed;         974 AA.
AC   Q94CG5;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Kinase-interacting protein 1 {ECO:0000303|PubMed:11500547};
GN   Name=KIP1 {ECO:0000303|PubMed:11500547};
OS   Petunia integrifolia (Violet-flowered petunia) (Salpiglossis integrifolia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4103 {ECO:0000312|EMBL:AAK40247.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PRK1, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11500547; DOI=10.1104/pp.126.4.1480;
RA   Skirpan A.L., McCubbin A.G., Ishimizu T., Wang X., Hu Y., Dowd P.E., Ma H.,
RA   Kao T.;
RT   "Isolation and characterization of kinase interacting protein 1, a pollen
RT   protein that interacts with the kinase domain of PRK1, a receptor-like
RT   kinase of petunia.";
RL   Plant Physiol. 126:1480-1492(2001).
RN   [2]
RP   DOMAIN.
RX   PubMed=22840520; DOI=10.1016/j.cub.2012.06.041;
RA   Deeks M.J., Calcutt J.R., Ingle E.K., Hawkins T.J., Chapman S.,
RA   Richardson A.C., Mentlak D.A., Dixon M.R., Cartwright F., Smertenko A.P.,
RA   Oparka K., Hussey P.J.;
RT   "A superfamily of actin-binding proteins at the actin-membrane nexus of
RT   higher plants.";
RL   Curr. Biol. 22:1595-1600(2012).
CC   -!- FUNCTION: Probably involved in the receptor-like kinase-mediated signal
CC       transduction pathway. {ECO:0000305|PubMed:11500547}.
CC   -!- SUBUNIT: Homodimer or homooligomer. Interacts with PRK1.
CC       {ECO:0000269|PubMed:11500547}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11500547}.
CC   -!- TISSUE SPECIFICITY: Expressed in mature pollen grains and pollen tubes,
CC       but not in style, ovary, petal, leaf, root or sepal.
CC       {ECO:0000269|PubMed:11500547}.
CC   -!- DEVELOPMENTAL STAGE: Detected around the time of microspore mitosis
CC       with a peak in mature pollen grains. {ECO:0000269|PubMed:11500547}.
CC   -!- DOMAIN: The NAB domain is capable to bind actin filaments.
CC       {ECO:0000269|PubMed:22840520}.
CC   -!- PTM: Phosphorylated by PRK1. {ECO:0000269|PubMed:11500547}.
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DR   EMBL; AY029758; AAK40247.1; -; mRNA.
DR   AlphaFoldDB; Q94CG5; -.
DR   SMR; Q94CG5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   InterPro; IPR011684; NAB.
DR   Pfam; PF07765; KIP1; 1.
DR   PROSITE; PS51774; NAB; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein.
FT   CHAIN           1..974
FT                   /note="Kinase-interacting protein 1"
FT                   /id="PRO_0000431905"
FT   DOMAIN          10..90
FT                   /note="NAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01110"
FT   REGION          151..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          173..423
FT                   /evidence="ECO:0000255"
FT   COILED          641..697
FT                   /evidence="ECO:0000255"
FT   COILED          784..807
FT                   /evidence="ECO:0000255"
FT   COILED          882..905
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   974 AA;  110425 MW;  25043EBD5998CBEF CRC64;
     MLQRAASNAY SWWAASHIRT KQSKWLEQSL HDMQGRVESV IKLIEEDGDS FAKRAEMYYK
     KRPELINFVE ESYRAYRALA ERYDHLSKEL QTANNTIATI FPEQIQLAMD EEDEYGAPKM
     PKDFLQMPAS GSNIPKVPPK APIKDLKGLM STASKQKQGK QSSKIEDAAK SGLSKNEAIE
     EIDKLQKDIL ALQTMKEFIR SSYQSSLEKF RGLENQIMEK QQKICELEDE FGEGRVIEDA
     EACTLMAEAA LQSCQETVTQ LQEKQESYTQ EAREEFKKIE DACNKLNSFR HKYLGDQIDE
     AKVYISPIQE VDKEIESLQE KIKDQIDATS KGSLTMSQLA EKIDELVNKV VSLETAVSSQ
     TLLLERFRAE ADELQAQVQT LEDDKAALTD THNLNIRVTA IEAKLQNIEN LNKDVVNQNS
     CLRTHFVEAR ANIDHLSDKL SSVQPDEEID GTDSSPDQVI ALAEIKLEEE SLKQKDHPSS
     AEGLKNLSTI KAEGPKNLST IKTEGPKSLS TIKAEGPKNL STIKAEGPKN LSTIKTEGPK
     SLSTIETEVP KNLSTIKTED KEVRKQQGSS TVVSDKKTTM KHVTFAQPTP AEKGDEKVSA
     QSGNTSVYET HTQKSAEKDD ELNWQQMLLS GLDDKENILL NEYTAILKNY KEVTKKLSDI
     EKKDRDTEFE LTLQTRELKS AIAKRDEEIH NLRQKLSLMQ QGNASENKAL KEELLDPSDP
     SSARGLKPED LPQIKDGDDE EDVKTILVDQ RATVSPLEGK LRMSIDAILD ENLDFWLRFS
     SAFHQIQKFK TTVHDLQNEI SKARDKEMQG NSPRVDVKSE IRPLYKHMKE IQNELTVWLE
     QTLSLKDELE RRFSALCSIQ EEISKGLKEE VEDETTFSSH QAAKFQGEVL NMKHENKKVR
     EELEAGISRV TILQEDVEKT VTQLDQEFGL TGNQSQLMQS VSKSRIPLQS FIFGTKPKKE
     KRSLFSRMNP NRKF