ID   A0A8M1KBV7_CLUHA        Unreviewed;       582 AA.
AC   A0A8M1KBV7;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   10-JUN-2026, entry version 19.
DE   SubName: Full=Kinesin-related protein 4-like {ECO:0000313|RefSeq:XP_042559970.1};
GN   Name=LOC122128989 {ECO:0000313|RefSeq:XP_042559970.1};
OS   Clupea harengus (Atlantic herring).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC   Clupeidae; Clupea.
OX   NCBI_TaxID=7950 {ECO:0000313|Proteomes:UP000515152, ECO:0000313|RefSeq:XP_042559970.1};
RN   [1] {ECO:0000313|RefSeq:XP_042559970.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2026) to UniProtKB.
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DR   RefSeq; XP_042559970.1; XM_042704036.1.
DR   AlphaFoldDB; A0A8M1KBV7; -.
DR   GeneID; 122128989; -.
DR   KEGG; char:122128989; -.
DR   OrthoDB; 299638at2759; -.
DR   Proteomes; UP000515152; Unplaced.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:TreeGrafter.
DR   GO; GO:0060271; P:cilium assembly; IEA:TreeGrafter.
DR   InterPro; IPR026205; PIBF1.
DR   PANTHER; PTHR18950:SF0; PROGESTERONE IMMUNOMODULATORY BINDING FACTOR 1; 1.
DR   PANTHER; PTHR18950; PROGESTERONE-INDUCED BLOCKING FACTOR 1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515152}.
FT   REGION          110..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          310..379
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          413..489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        110..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..164
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..214
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  66116 MW;  1501CEB0C88DFDEA CRC64;
     MWTLDPAMEE VLATILQGQR TLQGALLELC RQASADSSDE DQEEVVEKLT QGAEGLKVTT
     MLTAMNEEMQ LEAGYQPHGA ANTVQAWEAL PKMARTNERV FLGEFIDEND DDDVVDDVDY
     EGDVDDYDDE NADEIDDVDE NDYVHENHVN EDDEDDGDEE CDEAAVDKAV DENAADDCEN
     DHDESEEEVS LPKQAAPAKS APANATPAAP AKEAGMVKAK EESGEDDFDS QEVDDLESHR
     GQLKSFMESK TEEKERAVNA DKEMQAKHDQ LRQLQVGSDS RVAELSSQLK LKTFESERAQ
     MVQEETARSL SLCQMECEKH QKKLEVLTKE FYELQSSSEK RVVELQAQVS RQQVKLETYE
     RLEQELDDVT MQAAEMASEE EAERVLFSYG YDANVPTTAK RRLKQRVHLA RRVLQLEKQN
     THLRRDLEKQ NTQIGKVSKE LEAANQLIQQ AQQPYSYLNE TVKQRDCQIE KLKERITSLE
     EEVNVLKERT LKKAETDSKD VPEHAMLKSK RLYALPEVVD CFPEVTHVEL RKLEAKAHLN
     RQLALNSQEL STGERTEDGA DTDVVSSTQR EKRREKETNG RV
//