ID   TPX2_PATPE              Reviewed;         891 AA.
AC   E2RYF8;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Targeting protein for Xklp2 homolog;
DE            Short=TPX2 homolog {ECO:0000303|PubMed:21048162};
DE   AltName: Full=Microtubule-associated protein TPX2 homolog;
GN   Name=TPX2 {ECO:0000312|EMBL:BAJ24842.1};
OS   Patiria pectinifera (Starfish) (Asterina pectinifera).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Valvatacea; Valvatida; Asterinidae; Patiria.
OX   NCBI_TaxID=7594;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAJ24842.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=21048162; DOI=10.1242/jcs.076315;
RA   Abe Y., Okumura E., Hosoya T., Hirota T., Kishimoto T.;
RT   "A single starfish Aurora kinase performs the combined functions of Aurora-
RT   A and Aurora-B in human cells.";
RL   J. Cell Sci. 123:3978-3988(2010).
CC   -!- FUNCTION: Spindle assembly factor. Required for normal assembly of
CC       mitotic spindles (By similarity). {ECO:0000250|UniProtKB:A4IH24}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A4IH24}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:A4IH24}.
CC   -!- TISSUE SPECIFICITY: Detectable in immature oocytes.
CC       {ECO:0000269|PubMed:21048162}.
CC   -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB560815; BAJ24842.1; -; mRNA.
DR   AlphaFoldDB; E2RYF8; -.
DR   PRIDE; E2RYF8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0032147; P:activation of protein kinase activity; IEA:InterPro.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:InterPro.
DR   InterPro; IPR027329; TPX2_C.
DR   InterPro; IPR027330; TPX2_central_dom.
DR   InterPro; IPR009675; TPX2_fam.
DR   PANTHER; PTHR14326; PTHR14326; 1.
DR   Pfam; PF06886; TPX2; 1.
DR   Pfam; PF12214; TPX2_importin; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Nucleus.
FT   CHAIN           1..891
FT                   /note="Targeting protein for Xklp2 homolog"
FT                   /id="PRO_0000419527"
FT   REGION          42..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   891 AA;  101081 MW;  3BDBC58F5E35F99C CRC64;
     MADVEMMEYV DDVYEMDCPK FVDFSVPQVV DDNADEWFNF DHENGVPLTF DDKAVSPTAK
     ETPTSPLPQD PQESHSVIGH SETDTTLQES SAPEIATSEK QKYASPSDDV SSAESETCEM
     STDSMQDKPA VPESAVRNVT DDEATVQESS DAEETQTLPS SCVDSSTAEM STDSLEDKPQ
     KPQMQESPKP RKRYGNLVTS FARRDEDTTT ASSDHSEPEQ KKPRSRQRSV EVVSRPTRKS
     PRLHSRRSAE PTRLKRPSIT SQAVKRRSAN SALGHPRSRV LSTDQPISKR RKIGSEITPA
     GRPDAKKSCP KLKAKINLTM PTTPTLLKRN LAKPNTQLKT TEQMELDRIA QFQHKLAAIR
     KKSALSYKAV KESVPVAPVH AAVQPTRPEE FKFETDARLK SHTMETRKDT KNKDFVGNLR
     KYVPSPSKPQ GITKPRPFNF SDNRKRTHEE SFSGEKKGYE FKATALAVSQ FHTKTPDRFR
     SKPLSEQNKG PEPAHDRPKK AKLTQPMTPA LESRNRHRPV TAISQAQREE QELADMKNYK
     FKARPVDPRV MSNIAVGVKT VHHKEPTKPI GFDLEIEKRL LERETNKVQT EERYEFRARP
     LPAKILAGPV GIAEAKAAAV TIPKSPAFAL KERVKVYKEK EREKEKDSEH DNSHIIKARP
     ILHAGVPFMP NIQHKRTEPE PFSFDEKIQE SKARKEAKIQ ETLREEERAR QFRAQPLPDL
     TWCSGVPDKK VKPPTQMAPF SVAEKGAKQA EEWSKKMEEE IRDCKRMANA FKAKPANILY
     EEPFVPEKST KPMTDISNFS LNTERRAEDR KGYEQAKYER QLAQDTAQAQ REAEKEEELR
     QQISKQRADS IHKAKPVRHY KAVEVLPSTK PLTQPKTPKF SDRTRRSSHT S