ID A0A1S3RH12_SALSA Unreviewed; 367 AA.
AC A0A1S3RH12;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Lissencephaly-1 homolog B isoform X3 {ECO:0000313|RefSeq:XP_014051152.1};
GN Name=lis1b {ECO:0000313|RefSeq:XP_014051152.1};
GN Synonyms=lis1-2 {ECO:0000313|RefSeq:XP_014051152.1}, pafah1b1-2
GN {ECO:0000313|RefSeq:XP_014051152.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014051152.1};
RN [1] {ECO:0000313|RefSeq:XP_014051152.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014051152.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Can self-associate. Component of the cytosolic PAF-AH (I)
CC heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2
CC (alpha2) and PAFAH1B3 (alpha1) subunits. The catalytic activity of the
CC enzyme resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits,
CC whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer
CC formation is not essential for the catalytic activity (By similarity).
CC Interacts with dynein, dynactin, nde1 and ndel1.
CC {ECO:0000256|ARBA:ARBA00023793}.
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DR RefSeq; XP_014051152.1; XM_014195677.1.
DR AlphaFoldDB; A0A1S3RH12; -.
DR GeneID; 100195234; -.
DR CTD; 100195234; -.
DR OrthoDB; 1798470at2759; -.
DR Proteomes; UP000087266; Chromosome ssa04.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.960.30; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR017252; Dynein_regulator_LIS1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44129:SF20; LISSENCEPHALY-1 HOMOLOG B; 1.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 5.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..367
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010320970"
FT REPEAT 118..159
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 160..201
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 202..243
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 244..275
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 321..347
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 367 AA; 41283 MW; 48B9DC6F9789C81A CRC64;
MSGKDYQICC FLFLSLSLSL SLCVRNRAIA DYLRSNGYEE AYSTFKKEAE LDMNEELDKK
YAGLLEKKWT SVIRLQKKVM ELESKLNEAK EEITLGGPVA QKRDPKEWIP RPPERYALSG
HRSPVTRVIF HPVFSVMVTS SEDATIKVWD YEAGDFERTL KGHTDSVQDI SFDQTGKLLA
SCSADMTIKL WDFQGFECIR TMHGHDHNVS SVAIMPNGDH IVSASRDKTI KMWEVATGYC
VKTFTGHREW VRMVRPNQDG SLIASCSNDQ TVRVWVATSK ECKAELREHE HVVECIAWAP
DTAHPTILEA TSSESKKNGK SGPFLLSGSR DKTIKMWDIS TGMCLMTLVG HDNWVCVTCS
ILPLGGS
//
