ID A0A2Y9R1A4_TRIMA Unreviewed; 1660 AA.
AC A0A2Y9R1A4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Intersectin-2 isoform X1 {ECO:0000313|RefSeq:XP_023588177.1, ECO:0000313|RefSeq:XP_023588178.1};
GN Name=LOC101356968 {ECO:0000313|RefSeq:XP_023588177.1,
GN ECO:0000313|RefSeq:XP_023588178.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023588177.1};
RN [1] {ECO:0000313|RefSeq:XP_023588177.1, ECO:0000313|RefSeq:XP_023588178.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_023588177.1; XM_023732409.1.
DR RefSeq; XP_023588178.1; XM_023732410.1.
DR KEGG; tmu:101356968; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd08375; C2_Intersectin; 1.
DR CDD; cd00052; EH; 2.
DR CDD; cd13264; PH_ITSN; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11988; SH3_Intersectin2_1; 1.
DR CDD; cd11990; SH3_Intersectin2_2; 1.
DR CDD; cd11992; SH3_Intersectin2_3; 1.
DR CDD; cd11994; SH3_Intersectin2_4; 1.
DR CDD; cd11996; SH3_Intersectin2_5; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 5.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR035737; Intersectin-2_SH3_1.
DR InterPro; IPR035738; Intersectin-2_SH3_2.
DR InterPro; IPR035739; Intersectin-2_SH3_3.
DR InterPro; IPR035740; Intersectin-2_SH3_4.
DR InterPro; IPR035741; Intersectin-2_SH3_5.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46006:SF9; INTERSECTIN-2 ISOFORM X1; 1.
DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF16652; PH_13; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 5.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 22..110
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 54..89
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 245..334
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 278..313
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 722..783
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 861..919
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 944..1002
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1016..1080
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1090..1149
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1172..1358
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1397..1507
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1515..1631
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 220..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..551
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 586..641
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1660 AA; 188862 MW; A0CC1692CCBD8EAF CRC64;
MMAQLPTAMN GGPNMWAITS EERTKHDKQF DNLKPSGGYI TGDQARTFFL QSGLPAPVLA
EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPMVLP PVMKQPPMFS PLISARFGMG
SMPNLSIPQS LPPVAPITTP LSSVTSGTTL PPLMMPAPLV PSGSTSSLPN GTASLIQPLS
IPYSSSTLPH TSSYSLMMGG FGGASIQKAQ SLIDLGSSSS TSSTASLSGN SPKTGTSEWA
VPQPSRLKYR QKFNSLDKSM SGYLSGFQAR NALLQSNLSQ TQLATIWTLA DIDGDGQLKA
EEFILAMHLT DMAKAGQPLP LTLPPELVPP SFRGGKQLDS INGTLPSYQK IQEEEPQKKL
PVTFEDKWKA NYERGNMELE KRRQALMEQQ QREAERKAQK EKEEWERKQR ELQEQEWKKQ
LELEKRLEKQ RELERQREEE RRKEIERREA AKQELERQRR LEWERIRRQE LLNQRNREQE
EIVRLNSKKK SLHLELEALN GKHQQISGRL QDVRLRKQTQ KTELEVLDKQ CDLEIMEIKQ
LQQELQEYQN KLICLVPEKQ LLNERIKNMQ LDNTPDSGIS LLHKKSLEKE ELCQRLKEQL
DALEKETASK LSEMDSFNNQ LKELRESYNT QQLALEQLHK IKCDKLKEME RKRSEMIQKK
KLDDDAARKA KQGKENLWRE SLRKEEEEKQ KQLQEKKIQE KIQEEEQKAV EKQCKDKGGT
ASALVNYRAL YPFEARSHDE MSFNSGDIIQ VDEKTIGEPG WLYGSSKGNF GWFPCNYVEK
MSSSEKALSP KKALLPPAVS LPATSTSSEP LSSNQPASVT DYQNVSFSNL TVNTSWQKKS
AFTRTVSPAS VSPIHGQGQV VENLKAQALC SWTAKKDNHL NFSKHDIITV LEQQENWWFG
EVHGGRGWFP KSYVKIIPGS EVKREEPEAV YASVNKKPTS AAYTVGDEYI ALYSYSSVEP
GDLTFTEGEE ILVTQKDGEW WAGSIGARTG IFPSNYVKPK DQESFGSASK SGTSNKKPEI
AQVTSAYMAS GSEQLSLAPG QLILILKKNA SGWWQGELQA RGKKRQKGWF PASHVKLLGP
SSERTTPAFH PVCQVIAMYD YVANNEDELN FSKGQLINVL NKDDPDWWQG EINGVTGLFP
SNYVKMTTDS DPSQQWCADL QTLDTMQPIE RKRQGYIHEL IQTEERYMDD LQLVLEVFQK
RMAESGFLTE GEMALIFVNW KELIMSNTKL LKALRVRKKT GGEKMPVQMI GDILAAELSH
MQAYIRFCSC QLNGAALLQQ KTDEDTDFKE FLKKLASDPR CKGMPLSSFL LKPMQRITRY
PLLIRSILEN TLESHVDHSS LKLALERAEE LCSQVNEGVR EKENSDRLEW IQAHVQCEGL
AEQLIFNSLT NCLGPRKLLH SGKLYKTKSN KELHGFLFND FLLLTYMVKQ FAVSSGSEKL
FSSKSNAQFK MYKTPIFLNE VLVKLPTDPS SDEPVFHISH IDRVYTLRTD NINERTAWVQ
KIKAASEQYI DTEKKKREKA YQARSQKTSG IGRLMVHVIE ATELKACKPN GKSNPYCEIS
MGPQSYTTRT LQDTLNPKWN FNCQFFIKDL YQDVLCLTMF DRDQFSPDDF LGRTEVPVAK
IRTEQESKGP TTRRLLLHEV PTGEVWVRFD LQLFEQKNQL
//
