PAXB_DICDI
ID PAXB_DICDI Reviewed; 569 AA.
AC Q8MML5; O15817; Q555N0; Q8T166;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Paxillin-B;
GN Name=paxB; ORFNames=DDB_G0274109;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX3-1;
RX PubMed=16155255; DOI=10.1242/jcs.02557;
RA Bukharova T., Weijer G., Bosgraaf L., Dormann D., van Haastert P.J.,
RA Weijer C.J.;
RT "Paxillin is required for cell-substrate adhesion, cell sorting and slug
RT migration during Dictyostelium development.";
RL J. Cell Sci. 118:4295-4310(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Required for cell-substrate adhesion, cell sorting, slug
CC migration, and cell differentiation. May function upstream of limB.
CC {ECO:0000269|PubMed:16155255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16155255}. Cell projection, filopodium
CC {ECO:0000269|PubMed:16155255}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:16155255}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16155255}. Note=Expressed at the tips of filopodial
CC structures located at the trailing ends of cells. Found in the focal
CC adhesions at the cell-substrate interface.
CC -!- TISSUE SPECIFICITY: Expressed in the upper and lower cup of the
CC fruiting body. {ECO:0000269|PubMed:16155255}.
CC -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth and all stages
CC of development, with a peak during slug formation.
CC {ECO:0000269|PubMed:16155255}.
CC -!- DISRUPTION PHENOTYPE: Cells are less adhesive to the substrate and
CC remain competent to aggregate, although multicellular development is
CC severely impeded from the mound stage. They are defective in proper
CC cell type proportioning, cell sorting, slug migration and form
CC defective fruiting bodies. {ECO:0000269|PubMed:16155255}.
CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA05356.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ002382; CAA05356.1; ALT_FRAME; mRNA.
DR EMBL; AC123513; AAM44368.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL69947.1; -; Genomic_DNA.
DR RefSeq; XP_644036.1; XM_638944.1.
DR AlphaFoldDB; Q8MML5; -.
DR SMR; Q8MML5; -.
DR STRING; 44689.DDB0185208; -.
DR PaxDb; Q8MML5; -.
DR EnsemblProtists; EAL69947; EAL69947; DDB_G0274109.
DR GeneID; 8619466; -.
DR KEGG; ddi:DDB_G0274109; -.
DR dictyBase; DDB_G0274109; paxB.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_001357_1_2_1; -.
DR InParanoid; Q8MML5; -.
DR OMA; KPFEGGN; -.
DR PRO; PR:Q8MML5; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0032433; C:filopodium tip; IDA:dictyBase.
DR GO; GO:0005925; C:focal adhesion; IDA:dictyBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:dictyBase.
DR GO; GO:0016477; P:cell migration; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006897; P:endocytosis; IMP:dictyBase.
DR GO; GO:0061952; P:midbody abscission; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:dictyBase.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:dictyBase.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:dictyBase.
DR GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 4.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell projection; Cytoplasm; Cytoskeleton;
KW LIM domain; Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..569
FT /note="Paxillin-B"
FT /id="PRO_0000328171"
FT DOMAIN 334..391
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 393..452
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 453..510
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 511..569
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 62..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 10..18
FT /note="LD motif 1"
FT MOTIF 106..112
FT /note="LD motif 2"
FT MOTIF 232..239
FT /note="LD motif 3"
FT MOTIF 311..318
FT /note="LD motif 4"
FT COMPBIAS 133..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 40
FT /note="G -> R (in Ref. 1; CAA05356)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="Missing (in Ref. 1; CAA05356)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="A -> T (in Ref. 1; CAA05356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 62330 MW; D7592F9901BB222F CRC64;
MATKGLNMDD LDLLLADLGR PKSSIKVTAT VQTTATPSSG KNFDNSDIQN EIQSIIEELD
QQPQTVQTIS TPAPKNHNTT TTTASFSVSS QPAPQPPQQS QQIDGLDDLD ELMESLNTSI
STALKAVPTT PEEHITHANS NSPPPSLHKN TSSTNSASSL SRPNNNPSVV STPQPGKVTS
TATITTKKQP ALSKATLETT SGNNVYSSQP SQSQPQPYKV TATNSQPSSD DLDELLKGLS
PSTTTTTTVP PPVQRDQHQH HHQHQHHHHH NPNHNQTQTV TTQINIGRTN TPNNNNNNNT
NSPKVVHGDD LDNLLNNLTS QVKDIDSTGP TSRGTCGGCR KPIFGETIQA MGKFYHPEHF
CCHNCQNPLG TKNYYEQESL PHCEKCYQEL FCARCAHCDE PISDRCITAL GKKWHVHHFV
CTQCLKPFEG GNFFERDGRP YCEADFYSTF AVRCGGCNSP IRGECINALG TQWHPEHFVC
QYCQKSFTNG QFFEFGGKPY CDVHYHQQAG SVCSGCGKAV SGRCVDALDK KWHPEHFVCA
FCMNPLAGGS YTANNGKPYC KGCHNKLFA
